This drug entry is a stub and has not been fully annotated. It is scheduled to be annotated soon.
Identification
- Summary
Pyridoxal phosphate is a vitamin available in many formulations to correct vitamin B6 deficiency.
- Brand Names
- EnBrace HR, EnLyte
- Generic Name
- Pyridoxal phosphate
- DrugBank Accession Number
- DB00114
- Background
This is the active form of vitamin B6 serving as a coenzyme for synthesis of amino acids, neurotransmitters (serotonin, norepinephrine), sphingolipids, aminolevulinic acid. During transamination of amino acids, pyridoxal phosphate is transiently converted into pyridoxamine phosphate (pyridoxamine).
- Type
- Small Molecule
- Groups
- Approved, Investigational, Nutraceutical
- Structure
Structure for Pyridoxal phosphate (DB00114)
- Weight
- Average: 247.1419
Monoisotopic: 247.024573569 - Chemical Formula
- C8H10NO6P
- Synonyms
- 3-hydroxy-2-methyl-5-((phosphonooxy)methyl)-4-pyridinecarboxaldehyde
- 3-hydroxy-5-(hydroxymethyl)-2-methylisonicotinaldehyde 5-phosphate
- Codecarboxylase
- PLP
- Pyridoxal 5-monophosphoric acid ester
- Pyridoxal 5-phosphate
- Pyridoxal 5'-phosphate
- Pyridoxal P
- Pyridoxal phosphate anhydrous
- Pyridoxal-5P
- Pyridoxal-P
Pharmacology
- Indication
For nutritional supplementation and for treating dietary shortage or imbalance.
Reduce drug development failure ratesBuild, train, & validate machine-learning modelswith evidence-based and structured datasets.Build, train, & validate predictive machine-learning models with structured datasets.- Associated Conditions
Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Used in combination to treat Pernicious anemia Regimen in combination with: Citric acid (DB04272), Flavin adenine dinucleotide (DB03147), L-threonic acid (DB11192), Sodium citrate (DB09154), Leucovorin (DB00650), Betaine (DB06756), Phosphatidyl serine (DB00144), Levomefolic acid (DB11256), Ascorbic acid (DB00126), Folic acid (DB00158), Cobamamide (DB11191), NADH (DB00157) ••• ••••• Used in combination for prophylaxis of Vitamin b6 deficiency Combination Product in combination with: Pyridoxine (DB00165) •••••••••••• •••••••••• ••••••• •••••••••••• ••• •••••••• Used in combination to treat Vitamin b6 deficiency Combination Product in combination with: Pyridoxine (DB00165) •••••••••••• •••••••••• ••••••• •••••••••••• ••• •••••••• - Associated Therapies
- Contraindications & Blackbox Warnings
Prevent Adverse Drug Events TodayTap into our Clinical API for life-saving information on contraindications & blackbox warnings, population restrictions, harmful risks, & more.Avoid life-threatening adverse drug events with our Clinical API- Pharmacodynamics
The two major forms of vitamin B6 are pyridoxine and pyridoxamine. In the liver they are converted to pyridoxal phosphate (PLP) which is a cofactor in many reactions of amino acid metabolism. PLP also is necessary for the enzymatic reaction governing the release of glucose from glycogen. Pyroluria is one potential cause of vitamin B6 deficiency.
- Mechanism of action
Pyridoxal Phosphate is a coenzyme of many enzymatic reactions. It is the active form of vitamin B6 which comprises three natural organic compounds, pyridoxal, pyridoxamine and pyridoxine. Pyridoxal phosphate acts as a coenzyme in all transamination reactions, and in some oxylation and deamination reactions of amino acids. The aldehyde group of pyridoxal phosphate forms a Schiff-base linkage with the epsilon-amino group of a specific lysine group of the aminotransferase enzyme. The alpha-amino group of the amino acid substrate displaces the epsilon-amino group of the active-site lysine residue. The resulting aldimine becomes deprotonated to become a quinoid intermediate, which in turn accepts a proton at a different position to become a ketimine. Ketimine becomes hydrolyzed so that the amino group remains on the protein complex.
- Absorption
Not Available
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
- Not Available
- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
Improve decision support & research outcomesWith structured adverse effects data, including: blackbox warnings, adverse reactions, warning & precautions, & incidence rates. View sample adverse effects data in our new Data Library!Improve decision support & research outcomes with our structured adverse effects data.- Toxicity
Not Available
- Pathways
- Pharmacogenomic Effects/ADRs
- Not Available
Interactions
- Drug Interactions
- This information should not be interpreted without the help of a healthcare provider. If you believe you are experiencing an interaction, contact a healthcare provider immediately. The absence of an interaction does not necessarily mean no interactions exist.Not Available
- Food Interactions
- No interactions found.
Products
Drug product information from 10+ global regionsOur datasets provide approved product information including:dosage, form, labeller, route of administration, and marketing period.Access drug product information from over 10 global regions.- Product Ingredients
Ingredient UNII CAS InChI Key Pyridoxal phosphate hydrate 5V5IOJ8338 41468-25-1 CEEQUQSGVRRXQI-UHFFFAOYSA-N - International/Other Brands
- Biosechs / Himitan / Vitazechs
- Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image PramLyte Pyridoxal phosphate (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Citric acid monohydrate (1.83 mg/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Escitalopram oxalate (10 mg/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic acid (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (7 mg/1) + Magnesium ascorbate (24 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Sodium citrate (3.67 mg/1) + Zinc ascorbate (1 mg/1) Kit Oral Allegis Pharmaceuticals, LLC 2015-09-11 2016-01-04 US 
- Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image BumP DHA Pyridoxal phosphate (5 mg/1) + Cobamamide (500 mg/1) + Flavin adenine dinucleotide (1 mg/1) + Flavin mononucleotide (2 mg/1) + Iron (15 mg/1) + Leucovorin (1 mg/1) + Levomefolate magnesium (1 mg/1) + Magnesium oxide (125 mg/1) + NADH (25 ug/1) + Omega-3 fatty acids (300 mg/1) + Potassium Iodide (250 ug/1) + Pyridoxine hydrochloride (20 mg/1) + Zinc glycinate (15 1/1) Capsule Oral Centurion Labs 2017-03-24 2017-04-17 US Dyzbac Pyridoxal phosphate (12.5 mg/1) + Ascorbic acid (150 mg/1) + Cholecalciferol (0.0125 mg/1) + Leucovorin (1 mg/1) + Lipoic acid (125 mg/1) + Mecobalamin (1 mg/1) + Resveratrol (50 mg/1) + Ubidecarenone (50 mg/1) Tablet Oral Basiem 2015-10-28 2015-11-01 US Dyzbac Pyridoxal phosphate (12.5 mg/1) + Ascorbic acid (125 mg/1) + Cholecalciferol (500 [iU]/1) + Leucovorin (1 mg/1) + Lipoic acid (150 mg/1) + Mecobalamin (1 mg/1) + Resveratrol (50 mg/1) + Ubidecarenone (25 mg/1) Tablet Oral Basiem 2015-11-05 2016-01-01 US EnBrace HR Pyridoxal phosphate (25 ug/1) + 1,2-docosahexanoyl-sn-glycero-3-phosphoserine calcium (6.4 mg/1) + 1,2-icosapentoyl-sn-glycero-3-phosphoserine calcium (800 ug/1) + Betaine (500 ug/1) + Cobamamide (50 ug/1) + Cocarboxylase (25 ug/1) + Ferrous cysteine glycinate (13.6 mg/1) + Flavin adenine dinucleotide (25 ug/1) + Folic acid (1 mg/1) + Magnesium L-threonate (1 mg/1) + Leucovorin (2.5 mg/1) + Levomefolate magnesium (5.23 mg/1) + Magnesium ascorbate (24 mg/1) + NADH (25 ug/1) + Phosphatidyl serine (12 mg/1) + Zinc ascorbate (1 mg/1) Capsule, delayed release pellets Oral Jaymac Pharma 2011-08-12 Not applicable US L-Methyl-B6-B12 Pyridoxal phosphate (35 mg/1) + Levomefolate calcium (3 mg/1) + Mecobalamin (2 mg/1) Tablet Oral Seton Pharmaceuticals 2010-08-12 2012-06-30 US
Categories
- ATC Codes
- A11HA06 — Pyridoxal phosphate
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as pyridoxals and derivatives. These are compounds containing a pyridoxal moiety, which consists of a pyridine ring substituted at positions 2,3,4, and 5 by a methyl group, a hydroxyl group, a carbaldehyde group, and a hydroxymethyl group, respectively.
- Kingdom
- Organic compounds
- Super Class
- Organoheterocyclic compounds
- Class
- Pyridines and derivatives
- Sub Class
- Pyridine carboxaldehydes
- Direct Parent
- Pyridoxals and derivatives
- Alternative Parents
- Monoalkyl phosphates / Methylpyridines / Hydroxypyridines / Aryl-aldehydes / Vinylogous acids / Heteroaromatic compounds / Azacyclic compounds / Organopnictogen compounds / Organonitrogen compounds / Organic oxides show 1 more
- Substituents
- Aldehyde / Alkyl phosphate / Aromatic heteromonocyclic compound / Aryl-aldehyde / Azacycle / Heteroaromatic compound / Hydrocarbon derivative / Hydroxypyridine / Methylpyridine / Monoalkyl phosphate show 10 more
- Molecular Framework
- Aromatic heteromonocyclic compounds
- External Descriptors
- monohydroxypyridine, pyridinecarbaldehyde, methylpyridines, vitamin B6 phosphate (CHEBI:18405)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- F06SGE49M6
- CAS number
- 54-47-7
- InChI Key
- NGVDGCNFYWLIFO-UHFFFAOYSA-N
- InChI
- InChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
- IUPAC Name
- [(4-formyl-5-hydroxy-6-methylpyridin-3-yl)methoxy]phosphonic acid
- SMILES
- CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O
References
- Synthesis Reference
Robert C. Siegel, "Synthesis of cross-links in the helical domain of collagen using pyridoxal 5-phosphate and copper or iron." U.S. Patent US4544638, issued June, 1981.
US4544638- General References
- Not Available
- External Links
- Human Metabolome Database
- HMDB0001491
- KEGG Drug
- D00006
- KEGG Compound
- C00018
- PubChem Compound
- 1051
- PubChem Substance
- 46506428
- ChemSpider
- 1022
- BindingDB
- 50118216
- 9004
- ChEBI
- 18405
- ChEMBL
- CHEMBL82202
- ZINC
- ZINC000001532514
- Therapeutic Targets Database
- DNC001499
- PharmGKB
- PA164749650
- PDBe Ligand
- PLP
- PDRhealth
- PDRhealth Drug Page
- Wikipedia
- Pyridoxal_phosphate
- PDB Entries
- 1a3g / 1a50 / 1a5a / 1a5b / 1a5s / 1aam / 1aaw / 1ahe / 1ahf / 1ahg … show 1302 more
- MSDS
- Download (36.1 KB)
Clinical Trials
- Clinical Trials
Phase Status Purpose Conditions Count 4 Withdrawn Treatment Menstrual Related Mood Disorder / Premenstrual Dysphoric Disorder (PMDD) / Premenstrual Syndrome (PMS) / Premenstrual tension with edema 1 3 Completed Treatment Coronary Artery Bypass Grafting (CABG) / Myocardial Ischemia / Reperfusion Injury 1 3 Not Yet Recruiting Treatment Pyridox(am)Ine 5'-Phosphate Oxidase Deficiency 2 2 Terminated Treatment Tardive Dyskinesia (TD) 1 0 Completed Basic Science Receptor Blockade 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Pamlab LLC
- Physicians Total Care Inc.
- Red River Pharma Manufacturing
- Dosage Forms
Form Route Strength Injection, powder, for solution Intravenous Injection, powder, lyophilized, for solution Intramuscular Capsule, liquid filled Oral Capsule, delayed release pellets Oral Injection Intramuscular Tablet Oral Tablet, coated Oral Capsule Oral Kit Oral Tablet, film coated Oral Capsule, gelatin coated Oral - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 255 °C PhysProp water solubility Appreciable Not Available logP -1.2 Not Available - Predicted Properties
Property Value Source Water Solubility 5.7 mg/mL ALOGPS logP -0.55 ALOGPS logP -2.1 Chemaxon logS -1.6 ALOGPS pKa (Strongest Acidic) 1.68 Chemaxon pKa (Strongest Basic) 4.11 Chemaxon Physiological Charge -2 Chemaxon Hydrogen Acceptor Count 6 Chemaxon Hydrogen Donor Count 3 Chemaxon Polar Surface Area 116.95 Å2 Chemaxon Rotatable Bond Count 4 Chemaxon Refractivity 54.75 m3·mol-1 Chemaxon Polarizability 20.9 Å3 Chemaxon Number of Rings 1 Chemaxon Bioavailability 1 Chemaxon Rule of Five Yes Chemaxon Ghose Filter No Chemaxon Veber's Rule No Chemaxon MDDR-like Rule No Chemaxon - Predicted ADMET Features
Property Value Probability Human Intestinal Absorption + 0.5078 Blood Brain Barrier + 0.8022 Caco-2 permeable - 0.6476 P-glycoprotein substrate Non-substrate 0.6324 P-glycoprotein inhibitor I Non-inhibitor 0.9035 P-glycoprotein inhibitor II Non-inhibitor 0.9694 Renal organic cation transporter Non-inhibitor 0.882 CYP450 2C9 substrate Non-substrate 0.6828 CYP450 2D6 substrate Non-substrate 0.7978 CYP450 3A4 substrate Non-substrate 0.5915 CYP450 1A2 substrate Non-inhibitor 0.8704 CYP450 2C9 inhibitor Non-inhibitor 0.9041 CYP450 2D6 inhibitor Non-inhibitor 0.901 CYP450 2C19 inhibitor Non-inhibitor 0.8772 CYP450 3A4 inhibitor Non-inhibitor 0.9308 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9352 Ames test Non AMES toxic 0.6624 Carcinogenicity Non-carcinogens 0.8948 Biodegradation Ready biodegradable 0.5443 Rat acute toxicity 1.6531 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.8729 hERG inhibition (predictor II) Non-inhibitor 0.9128
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 156.8800714 predictedDarkChem Lite v0.1.0 [M-H]- 156.7494714 predictedDarkChem Lite v0.1.0 [M-H]- 158.4545714 predictedDarkChem Lite v0.1.0 [M-H]- 158.3766714 predictedDarkChem Lite v0.1.0 [M-H]- 145.28539 predictedDeepCCS 1.0 (2019) [M+H]+ 157.1515714 predictedDarkChem Lite v0.1.0 [M+H]+ 157.1592714 predictedDarkChem Lite v0.1.0 [M+H]+ 157.8705714 predictedDarkChem Lite v0.1.0 [M+H]+ 157.6856714 predictedDarkChem Lite v0.1.0 [M+H]+ 147.64339 predictedDeepCCS 1.0 (2019) [M+Na]+ 157.0115714 predictedDarkChem Lite v0.1.0 [M+Na]+ 157.2108714 predictedDarkChem Lite v0.1.0 [M+Na]+ 156.9695714 predictedDarkChem Lite v0.1.0 [M+Na]+ 157.2723714 predictedDarkChem Lite v0.1.0 [M+Na]+ 154.76637 predictedDeepCCS 1.0 (2019)
Targets
Build, predict & validate machine-learning models
Use our structured and evidence-based datasets to unlock newinsights and accelerate drug research.
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and th...
- Gene Name
- AGXT2
- Uniprot ID
- Q9BYV1
- Uniprot Name
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Molecular Weight
- 57155.905 Da
References
- Lee IS, Muragaki Y, Ideguchi T, Hase T, Tsuji M, Ooshima A, Okuno E, Kido R: Molecular cloning and sequencing of a cDNA encoding alanine-glyoxylate aminotransferase 2 from rat kidney. J Biochem. 1995 Apr;117(4):856-62. [Article]
- Takada Y, Mori T, Noguchi T: The effect of vitamin B6 deficiency on alanine: glyoxylate aminotransferase isoenzymes in rat liver. Arch Biochem Biophys. 1984 Feb 15;229(1):1-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the production of GABA.
- Gene Name
- GAD1
- Uniprot ID
- Q99259
- Uniprot Name
- Glutamate decarboxylase 1
- Molecular Weight
- 66896.065 Da
References
- Hwang IK, Yoo KY, Kim DS, Eum WS, Park JK, Park J, Kwon OS, Kang TC, Choi SY, Won MH: Changes of pyridoxal kinase expression and activity in the gerbil hippocampus following transient forebrain ischemia. Neuroscience. 2004;128(3):511-8. [Article]
- Rust E, Martin DL, Chen CH: Cofactor and tryptophan accessibility and unfolding of brain glutamate decarboxylase. Arch Biochem Biophys. 2001 Aug 15;392(2):333-40. [Article]
- Jin H, Sha D, Wei J, Davis KM, Wu H, Jin Y, Wu JY: Effect of apocalmodulin on recombinant human brain glutamic acid decarboxylase. J Neurochem. 2005 Feb;92(4):739-48. [Article]
- Chen CH, Battaglioli G, Martin DL, Hobart SA, Colon W: Distinctive interactions in the holoenzyme formation for two isoforms of glutamate decarboxylase. Biochim Biophys Acta. 2003 Jan 31;1645(1):63-71. [Article]
- Tong JC, Mackay IR, Chin J, Law RH, Fayad K, Rowley MJ: Enzymatic characterization of a recombinant isoform hybrid of glutamic acid decarboxylase (rGAD67/65) expressed in yeast. J Biotechnol. 2002 Aug 7;97(2):183-90. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Ubiquitin protein ligase binding
- Specific Function
- Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, th...
- Gene Name
- CBS
- Uniprot ID
- P35520
- Uniprot Name
- Cystathionine beta-synthase
- Molecular Weight
- 60586.05 Da
References
- Taoka S, Banerjee R: Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine beta-synthase. J Biol Chem. 2002 Jun 21;277(25):22421-5. Epub 2002 Apr 10. [Article]
- Taoka S, Lepore BW, Kabil O, Ojha S, Ringe D, Banerjee R: Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry. 2002 Aug 20;41(33):10454-61. [Article]
- Mino K, Ishikawa K: Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1. J Bacteriol. 2003 Apr;185(7):2277-84. [Article]
- Evande R, Ojha S, Banerjee R: Visualization of PLP-bound intermediates in hemeless variants of human cystathionine beta-synthase: evidence that lysine 119 is a general base. Arch Biochem Biophys. 2004 Jul 15;427(2):188-96. [Article]
- Linnebank M, Janosik M, Kozich V, Pronicka E, Kubalska J, Sokolova J, Linnebank A, Schmidt E, Leyendecker C, Klockgether T, Kraus JP, Koch HG: The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: Vitamin B6 nonresponsiveness and a common ancestral haplotype. Hum Mutat. 2004 Oct;24(4):352-3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hyd...
- Gene Name
- KYNU
- Uniprot ID
- Q16719
- Uniprot Name
- Kynureninase
- Molecular Weight
- 52351.14 Da
References
- Momany C, Levdikov V, Blagova L, Lima S, Phillips RS: Three-dimensional structure of kynureninase from Pseudomonas fluorescens. Biochemistry. 2004 Feb 10;43(5):1193-203. [Article]
- Rooseboom M, Vermeulen NP, Groot EJ, Commandeur JN: Tissue distribution of cytosolic beta-elimination reactions of selenocysteine Se-conjugates in rat and human. Chem Biol Interact. 2002 Aug 15;140(3):243-64. [Article]
- Lima S, Khristoforov R, Momany C, Phillips RS: Crystal structure of Homo sapiens kynureninase. Biochemistry. 2007 Mar 13;46(10):2735-44. Epub 2007 Feb 15. [Article]
- Walsh HA, Botting NP: Purification and biochemical characterization of some of the properties of recombinant human kynureninase. Eur J Biochem. 2002 Apr;269(8):2069-74. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Serine binding
- Specific Function
- Interconversion of serine and glycine.
- Gene Name
- SHMT1
- Uniprot ID
- P34896
- Uniprot Name
- Serine hydroxymethyltransferase, cytosolic
- Molecular Weight
- 53082.18 Da
References
- Trakatellis A, Dimitriadou A, Exindari M, Christodoulou D, Malissiovas N, Antoniadis A, Haitoglou K: Effect of combination of deoxypyridoxine with known anti-proliferative or immunosuppressive agents on lymphocyte serine hydroxymethyltransferase. Postgrad Med J. 1994;70 Suppl 1:S89-92. [Article]
- Jagath JR, Sharma B, Rao NA, Savithri HS: The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J Biol Chem. 1997 Sep 26;272(39):24355-62. [Article]
- Bourguignon J, Neuburger M, Douce R: Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase. Biochem J. 1988 Oct 1;255(1):169-78. [Article]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofac...
- Gene Name
- NFS1
- Uniprot ID
- Q9Y697
- Uniprot Name
- Cysteine desulfurase, mitochondrial
- Molecular Weight
- 50195.21 Da
References
- Ollagnier-De-Choudens S, Mulliez E, Hewitson KS, Fontecave M: Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase. Biochemistry. 2002 Jul 23;41(29):9145-52. [Article]
- You D, Wang L, Yao F, Zhou X, Deng Z: A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans. Biochemistry. 2007 May 22;46(20):6126-33. Epub 2007 May 1. [Article]
- Forlani F, Cereda A, Freuer A, Nimtz M, Leimkuhler S, Pagani S: The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form. FEBS Lett. 2005 Dec 19;579(30):6786-90. Epub 2005 Nov 21. [Article]
- Cupp-Vickery JR, Urbina H, Vickery LE: Crystal structure of IscS, a cysteine desulfurase from Escherichia coli. J Mol Biol. 2003 Jul 25;330(5):1049-59. [Article]
- Frazzon J, Fick JR, Dean DR: Biosynthesis of iron-sulphur clusters is a complex and highly conserved process. Biochem Soc Trans. 2002 Aug;30(4):680-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Activator
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a sca...
- Gene Name
- GOT1
- Uniprot ID
- P17174
- Uniprot Name
- Aspartate aminotransferase, cytoplasmic
- Molecular Weight
- 46247.14 Da
References
- Hansen CM, Shultz TD: Stability of vitamin B-6-dependent aminotransferase activity in frozen packed erythrocytes is dependent on storage temperature. J Nutr. 2001 May;131(5):1581-3. [Article]
- Eliot AC, Kirsch JF: Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues. Biochemistry. 2002 Mar 19;41(11):3836-42. [Article]
- Cooper AJ, Bruschi SA, Anders MW: Toxic, halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem Pharmacol. 2002 Aug 15;64(4):553-64. [Article]
- Waldmann A, Dorr B, Koschizke JW, Leitzmann C, Hahn A: Dietary intake of vitamin B6 and concentration of vitamin B6 in blood samples of German vegans. Public Health Nutr. 2006 Sep;9(6):779-84. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- OAT
- Uniprot ID
- P04181
- Uniprot Name
- Ornithine aminotransferase, mitochondrial
- Molecular Weight
- 48534.39 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Protein homodimerization activity
- Specific Function
- Key enzyme of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine.
- Gene Name
- ODC1
- Uniprot ID
- P11926
- Uniprot Name
- Ornithine decarboxylase
- Molecular Weight
- 51147.73 Da
References
- Jackson LK, Goldsmith EJ, Phillips MA: X-ray structure determination of Trypanosoma brucei ornithine decarboxylase bound to D-ornithine and to G418: insights into substrate binding and ODC conformational flexibility. J Biol Chem. 2003 Jun 13;278(24):22037-43. Epub 2003 Apr 2. [Article]
- Jackson LK, Brooks HB, Myers DP, Phillips MA: Ornithine decarboxylase promotes catalysis by binding the carboxylate in a buried pocket containing phenylalanine 397. Biochemistry. 2003 Mar 18;42(10):2933-40. [Article]
- Jackson LK, Baldwin J, Akella R, Goldsmith EJ, Phillips MA: Multiple active site conformations revealed by distant site mutation in ornithine decarboxylase. Biochemistry. 2004 Oct 19;43(41):12990-9. [Article]
- Khomutov AR: Inhibition of enzymes of polyamine biosynthesis by substrate-like O-substituted hydroxylamines. Biochemistry (Mosc). 2002 Oct;67(10):1159-67. [Article]
- Myers DP, Jackson LK, Ipe VG, Murphy GE, Phillips MA: Long-range interactions in the dimer interface of ornithine decarboxylase are important for enzyme function. Biochemistry. 2001 Nov 6;40(44):13230-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykyn...
- Gene Name
- AADAT
- Uniprot ID
- Q8N5Z0
- Uniprot Name
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Molecular Weight
- 47351.17 Da
References
- Goh DL, Patel A, Thomas GH, Salomons GS, Schor DS, Jakobs C, Geraghty MT: Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT). Mol Genet Metab. 2002 Jul;76(3):172-80. [Article]
- Cooper AJ: The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants. Neurochem Int. 2004 Jun;44(8):557-77. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Succinate-semialdehyde dehydrogenase binding
- Specific Function
- Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-al...
- Gene Name
- ABAT
- Uniprot ID
- P80404
- Uniprot Name
- 4-aminobutyrate aminotransferase, mitochondrial
- Molecular Weight
- 56438.405 Da
References
- Storici P, De Biase D, Bossa F, Bruno S, Mozzarelli A, Peneff C, Silverman RB, Schirmer T: Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin. J Biol Chem. 2004 Jan 2;279(1):363-73. Epub 2003 Oct 8. [Article]
- Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [Article]
- Sulaiman SA, Suliman FE, Barghouthi S: Kinetic studies on the inhibition of GABA-T by gamma-vinyl GABA and taurine. J Enzyme Inhib Med Chem. 2003 Aug;18(4):297-301. [Article]
- Markova M, Peneff C, Hewlins MJ, Schirmer T, John RA: Determinants of substrate specificity in omega-aminotransferases. J Biol Chem. 2005 Oct 28;280(43):36409-16. Epub 2005 Aug 11. [Article]
- Liu W, Peterson PE, Langston JA, Jin X, Zhou X, Fisher AJ, Toney MD: Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry. 2005 Mar 1;44(8):2982-92. [Article]
- Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxamine-phosphate oxidase activity
- Specific Function
- Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
- Gene Name
- PNPO
- Uniprot ID
- Q9NVS9
- Uniprot Name
- Pyridoxine-5'-phosphate oxidase
- Molecular Weight
- 29987.79 Da
References
- Gospe SM Jr: Pyridoxine-dependent seizures: new genetic and biochemical clues to help with diagnosis and treatment. Curr Opin Neurol. 2006 Apr;19(2):148-53. [Article]
- Hwang IK, Kim DW, Jung JY, Yoo KY, Cho JH, Kwon OS, Kang TC, Choi SY, Kim YS, Won MH: Age-dependent changes of pyridoxal phosphate synthesizing enzymes immunoreactivities and activities in the gerbil hippocampal CA1 region. Mech Ageing Dev. 2005 Dec;126(12):1322-30. Epub 2005 Oct 3. [Article]
- Pearl PL, Hartka TR, Taylor J: Diagnosis and treatment of neurotransmitter disorders. Curr Treat Options Neurol. 2006 Nov;8(6):441-50. [Article]
- Hoffmann GF, Schmitt B, Windfuhr M, Wagner N, Strehl H, Bagci S, Franz AR, Mills PB, Clayton PT, Baumgartner MR, Steinmann B, Bast T, Wolf NI, Zschocke J: Pyridoxal 5'-phosphate may be curative in early-onset epileptic encephalopathy. J Inherit Metab Dis. 2007 Feb;30(1):96-9. Epub 2006 Dec 23. [Article]
- Mills PB, Surtees RA, Champion MP, Beesley CE, Dalton N, Scambler PJ, Heales SJ, Briddon A, Scheimberg I, Hoffmann GF, Zschocke J, Clayton PT: Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase. Hum Mol Genet. 2005 Apr 15;14(8):1077-86. Epub 2005 Mar 16. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Sphinganine-1-phosphate aldolase activity
- Specific Function
- Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis.
- Gene Name
- SGPL1
- Uniprot ID
- O95470
- Uniprot Name
- Sphingosine-1-phosphate lyase 1
- Molecular Weight
- 63523.265 Da
References
- Ikeda M, Kihara A, Igarashi Y: Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5'-phosphate binding domain exposed to the cytosol. Biochem Biophys Res Commun. 2004 Dec 3;325(1):338-43. [Article]
- Bobbin RP: PPADS, an ATP antagonist, attenuates the effects of a moderately intense sound on cochlear mechanics. Hear Res. 2001 Jun;156(1-2):10-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has...
- Gene Name
- TAT
- Uniprot ID
- P17735
- Uniprot Name
- Tyrosine aminotransferase
- Molecular Weight
- 50398.895 Da
References
- Biagini MR, Tozzi A, Marcucci R, Paniccia R, Fedi S, Milani S, Galli A, Ceni E, Capanni M, Manta R, Abbate R, Surrenti C: Hyperhomocysteinemia and hypercoagulability in primary biliary cirrhosis. World J Gastroenterol. 2006 Mar 14;12(10):1607-12. [Article]
- Clayton TA, Lindon JC, Everett JR, Charuel C, Hanton G, Le Net JL, Provost JP, Nicholson JK: Hepatotoxin-induced hypertyrosinemia and its toxicological significance. Arch Toxicol. 2007 Mar;81(3):201-10. Epub 2006 Aug 11. [Article]
- Kim SY, An JJ, Kim DW, Choi SH, Lee SH, Hwang SI, Kwon OS, Kang TC, Won MH, Cho SW, Park J, Eum WS, Lee KS, Choi SY: Tat-mediated protein transduction of human brain pyridoxine-5-P oxidase into PC12 cells. J Biochem Mol Biol. 2006 Jan 31;39(1):76-83. [Article]
- Shaffer WA, Luong TN, Rothman SC, Kirsch JF: Quantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase. Protein Sci. 2002 Dec;11(12):2848-59. [Article]
- Venhorst J, ter Laak AM, Meijer M, van de Wetering I, Commandeur JN, Rooseboom M, Vermeulen NP: Modeling and molecular dynamics of glutamine transaminase K/cysteine conjugate beta-lyase. J Mol Graph Model. 2003 Sep;22(1):55-70. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Transaminase activity
- Specific Function
- Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to ...
- Gene Name
- CCBL1
- Uniprot ID
- Q16773
- Uniprot Name
- Kynurenine--oxoglutarate transaminase 1
- Molecular Weight
- 47874.765 Da
References
- Cooper AJ, Bruschi SA, Anders MW: Toxic, halogenated cysteine S-conjugates and targeting of mitochondrial enzymes of energy metabolism. Biochem Pharmacol. 2002 Aug 15;64(4):553-64. [Article]
- Mosca M, Croci C, Mostardini M, Breton J, Malyszko J, Avanzi N, Toma S, Benatti L, Gatti S: Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs. Biochim Biophys Acta. 2003 Jul 9;1628(1):1-10. [Article]
- Zhang L, Cooper AJ, Krasnikov BF, Xu H, Bubber P, Pinto JT, Gibson GE, Hanigan MH: Cisplatin-induced toxicity is associated with platinum deposition in mouse kidney mitochondria in vivo and with selective inactivation of the alpha-ketoglutarate dehydrogenase complex in LLC-PK1 cells. Biochemistry. 2006 Jul 25;45(29):8959-71. [Article]
- Venhorst J, ter Laak AM, Meijer M, van de Wetering I, Commandeur JN, Rooseboom M, Vermeulen NP: Modeling and molecular dynamics of glutamine transaminase K/cysteine conjugate beta-lyase. J Mol Graph Model. 2003 Sep;22(1):55-70. [Article]
- Cooper AJ, Pinto JT: Cysteine S-conjugate beta-lyases. Amino Acids. 2006 Feb;30(1):1-15. Epub 2006 Feb 6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Vitamin binding
- Specific Function
- Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
- Gene Name
- PYGL
- Uniprot ID
- P06737
- Uniprot Name
- Glycogen phosphorylase, liver form
- Molecular Weight
- 97147.82 Da
References
- Beauchamp NJ, Taybert J, Champion MP, Layet V, Heinz-Erian P, Dalton A, Tanner MS, Pronicka E, Sharrard MJ: High frequency of missense mutations in glycogen storage disease type VI. J Inherit Metab Dis. 2007 Oct;30(5):722-34. Epub 2007 Aug 21. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Serine c-palmitoyltransferase activity
- Specific Function
- Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate ...
- Gene Name
- SPTLC2
- Uniprot ID
- O15270
- Uniprot Name
- Serine palmitoyltransferase 2
- Molecular Weight
- 62923.765 Da
References
- Hanada K: Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. [Article]
- Tamura K, Mitsuhashi N, Hara-Nishimura I, Imai H: Characterization of an Arabidopsis cDNA encoding a subunit of serine palmitoyltransferase, the initial enzyme in sphingolipid biosynthesis. Plant Cell Physiol. 2001 Nov;42(11):1274-81. [Article]
- Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM: Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. Epub 2002 Jan 7. [Article]
- Ikushiro H, Hayashi H, Kagamiyama H: A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction. J Biol Chem. 2001 May 25;276(21):18249-56. Epub 2001 Mar 12. [Article]
- Tamura K, Nishiura H, Mori J, Imai H: Cloning and characterization of a cDNA encoding serine palmitoyltransferase in Arabidopsis thaliana. Biochem Soc Trans. 2000 Dec;28(6):745-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Sulfinoalanine decarboxylase activity
- Specific Function
- Not Available
- Gene Name
- CSAD
- Uniprot ID
- Q9Y600
- Uniprot Name
- Cysteine sulfinic acid decarboxylase
- Molecular Weight
- 55022.79 Da
References
- Skoldberg F, Rorsman F, Perheentupa J, Landin-Olsson M, Husebye ES, Gustafsson J, Kampe O: Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease. J Clin Endocrinol Metab. 2004 Apr;89(4):1636-40. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the biosynthesis of histamine from histidine.
- Gene Name
- HDC
- Uniprot ID
- P19113
- Uniprot Name
- Histidine decarboxylase
- Molecular Weight
- 74139.825 Da
References
- Skoldberg F, Portela-Gomes GM, Grimelius L, Nilsson G, Perheentupa J, Betterle C, Husebye ES, Gustafsson J, Ronnblom A, Rorsman F, Kampe O: Histidine decarboxylase, a pyridoxal phosphate-dependent enzyme, is an autoantigen of gastric enterochromaffin-like cells. J Clin Endocrinol Metab. 2003 Apr;88(4):1445-52. [Article]
- Moya-Garcia AA, Pino-Angeles A, Sanchez-Jimenez F: New structural insights to help in the search for selective inhibitors of mammalian pyridoxal 5'-phosphate-dependent histidine decarboxylase . 4. Synthesis, metabolism and release of histamine. Inflamm Res. 2006 Apr;55 Suppl 1:S55-6. [Article]
- Landete JM, Pardo I, Ferrer S: Histamine, histidine, and growth-phase mediated regulation of the histidine decarboxylase gene in lactic acid bacteria isolated from wine. FEMS Microbiol Lett. 2006 Jul;260(1):84-90. [Article]
- Skoldberg F, Rorsman F, Perheentupa J, Landin-Olsson M, Husebye ES, Gustafsson J, Kampe O: Analysis of antibody reactivity against cysteine sulfinic acid decarboxylase, a pyridoxal phosphate-dependent enzyme, in endocrine autoimmune disease. J Clin Endocrinol Metab. 2004 Apr;89(4):1636-40. [Article]
- Graham DE, Xu H, White RH: Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem. 2002 Jun 28;277(26):23500-7. Epub 2002 Apr 29. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Putrescine transmembrane transporter activity
- Specific Function
- Antizyme inhibitor protein that positively regulates ornithine decarboxylase (ODC) activity and polyamine uptake by counteracting the negative effect of antizymes OAZ1, OAZ2 and OAZ3 on ODC1 activi...
- Gene Name
- AZIN2
- Uniprot ID
- Q96A70
- Uniprot Name
- Antizyme inhibitor 2
- Molecular Weight
- 49979.185 Da
References
- Graham DE, Xu H, White RH: Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem. 2002 Jun 28;277(26):23500-7. Epub 2002 Apr 29. [Article]
- Patel CN, Adcock RS, Sell KG, Oliveira MA: Crystallization, X-ray diffraction and oligomeric characterization of arginine decarboxylase from Yersinia pestis, a key polyamine biosynthetic enzyme. Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2396-8. Epub 2004 Nov 26. [Article]
- Kidron H, Repo S, Johnson MS, Salminen TA: Functional classification of amino acid decarboxylases from the alanine racemase structural family by phylogenetic studies. Mol Biol Evol. 2007 Jan;24(1):79-89. Epub 2006 Sep 22. [Article]
- Arena ME, Manca de Nadra MC: Biogenic amine production by Lactobacillus. J Appl Microbiol. 2001 Feb;90(2):158-62. [Article]
- Shah R, Akella R, Goldsmith EJ, Phillips MA: X-ray structure of Paramecium bursaria Chlorella virus arginine decarboxylase: insight into the structural basis for substrate specificity. Biochemistry. 2007 Mar 13;46(10):2831-41. Epub 2007 Feb 17. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- SDS
- Uniprot ID
- P20132
- Uniprot Name
- L-serine dehydratase/L-threonine deaminase
- Molecular Weight
- 34625.105 Da
References
- Sun L, Bartlam M, Liu Y, Pang H, Rao Z: Crystal structure of the pyridoxal-5'-phosphate-dependent serine dehydratase from human liver. Protein Sci. 2005 Mar;14(3):791-8. Epub 2005 Feb 2. [Article]
- Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, Takusagawa F: Crystal structure of serine dehydratase from rat liver. Biochemistry. 2003 Nov 11;42(44):12854-65. [Article]
- Sun L, Li X, Dong Y, Yang M, Liu Y, Han X, Zhang X, Pang H, Rao Z: Crystallization and preliminary crystallographic analysis of human serine dehydratase. Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2297-9. Epub 2003 Nov 27. [Article]
- Ogawa H, Gomi T, Nishizawa M, Hayakawa Y, Endo S, Hayashi K, Ochiai H, Takusagawa F, Pitot HC, Mori H, Sakurai H, Koizumi K, Saiki I, Oda H, Fujishita T, Miwa T, Maruyama M, Kobayashi M: Enzymatic and biochemical properties of a novel human serine dehydratase isoform. Biochim Biophys Acta. 2006 May;1764(5):961-71. Epub 2006 Mar 20. [Article]
- Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, Booker SJ: Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. J Biol Chem. 2004 Jul 30;279(31):32418-25. Epub 2004 May 19. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- GCAT
- Uniprot ID
- O75600
- Uniprot Name
- 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial
- Molecular Weight
- 45284.6 Da
References
- Schmidt A, Sivaraman J, Li Y, Larocque R, Barbosa JA, Smith C, Matte A, Schrag JD, Cygler M: Three-dimensional structure of 2-amino-3-ketobutyrate CoA ligase from Escherichia coli complexed with a PLP-substrate intermediate: inferred reaction mechanism. Biochemistry. 2001 May 1;40(17):5151-60. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Lyase activity
- Specific Function
- The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the rem...
- Gene Name
- GLDC
- Uniprot ID
- P23378
- Uniprot Name
- Glycine dehydrogenase (decarboxylating), mitochondrial
- Molecular Weight
- 112728.805 Da
References
- Nakai T, Nakagawa N, Maoka N, Masui R, Kuramitsu S, Kamiya N: Structure of P-protein of the glycine cleavage system: implications for nonketotic hyperglycinemia. EMBO J. 2005 Apr 20;24(8):1523-36. Epub 2005 Mar 24. [Article]
- Igamberdiev AU, Ivlev AA, Bykova NV, Threlkeld CN, Lea PJ, Gardestrom P: Decarboxylation of glycine contributes to carbon isotope fractionation in photosynthetic organisms. Photosynth Res. 2001;67(3):177-84. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting wi...
- Gene Name
- GPT
- Uniprot ID
- P24298
- Uniprot Name
- Alanine aminotransferase 1
- Molecular Weight
- 54636.415 Da
References
- Cheung PY, Fong CC, Ng KT, Lam WC, Leung YC, Tsang CW, Yang M, Wong MS: Interaction between pyridoxal kinase and pyridoxal-5-phosphate-dependent enzymes. J Biochem. 2003 Nov;134(5):731-8. [Article]
- Halfon P, Imbert-Bismut F, Messous D, Antoniotti G, Benchetrit D, Cart-Lamy P, Delaporte G, Doutheau D, Klump T, Sala M, Thibaud D, Trepo E, Thabut D, Myers RP, Poynard T: A prospective assessment of the inter-laboratory variability of biochemical markers of fibrosis (FibroTest) and activity (ActiTest) in patients with chronic liver disease. Comp Hepatol. 2002 Dec 30;1(1):3. [Article]
- Inubushi T, Takasawa T, Tuboi Y, Watanabe N, Aki K, Katunuma N: Changes of glucose metabolism and skin-collagen neogenesis in vitamin B6 deficiency. Biofactors. 2005;23(2):59-67. [Article]
- Baines CJ, McKeown-Eyssen GE, Riley N, Cole DE, Marshall L, Loescher B, Jazmaji V: Case-control study of multiple chemical sensitivity, comparing haematology, biochemistry, vitamins and serum volatile organic compound measures. Occup Med (Lond). 2004 Sep;54(6):408-18. Epub 2004 Sep 3. [Article]
- Beranek M, Drsata J, Palicka V: Inhibitory effect of glycation on catalytic activity of alanine aminotransferase. Mol Cell Biochem. 2001 Feb;218(1-2):35-9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- O-phospho-l-serine:2-oxoglutarate aminotransferase activity
- Specific Function
- Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
- Gene Name
- PSAT1
- Uniprot ID
- Q9Y617
- Uniprot Name
- Phosphoserine aminotransferase
- Molecular Weight
- 40422.355 Da
References
- Battchikova N, Himanen JP, Ahjolahti M, Korpela T: Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing. Biochim Biophys Acta. 1996 Jul 18;1295(2):187-94. [Article]
- Hester G, Stark W, Moser M, Kallen J, Markovic-Housley Z, Jansonius JN: Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate. J Mol Biol. 1999 Feb 26;286(3):829-50. [Article]
- Kapetaniou EG, Thanassoulas A, Dubnovitsky AP, Nounesis G, Papageorgiou AC: Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies. Proteins. 2006 Jun 1;63(4):742-53. [Article]
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- ALAS1
- Uniprot ID
- P13196
- Uniprot Name
- 5-aminolevulinate synthase, nonspecific, mitochondrial
- Molecular Weight
- 70580.325 Da
References
- Nakamura I, Isobe N, Nakamura N, Kamihara T, Fukui S: Mechanism of thiamine-induced respiratory deficiency in Saccharomyces carlsbergensis. J Bacteriol. 1981 Sep;147(3):954-61. [Article]
- Harigae H, Furuyama K, Kudo K, Hayashi N, Yamamoto M, Sassa S, Sasaki T: A novel mutation of the erythroid-specific gamma-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. Am J Hematol. 1999 Oct;62(2):112-4. [Article]
- Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF: 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):361-6. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Transaminase activity
- Specific Function
- Not Available
- Gene Name
- AGXT
- Uniprot ID
- P21549
- Uniprot Name
- Serine--pyruvate aminotransferase
- Molecular Weight
- 43009.535 Da
References
- Coulter-Mackie MB, Lian Q: Consequences of missense mutations for dimerization and turnover of alanine:glyoxylate aminotransferase: study of a spectrum of mutations. Mol Genet Metab. 2006 Dec;89(4):349-59. Epub 2006 Sep 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphatase activity
- Specific Function
- Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization...
- Gene Name
- PDXP
- Uniprot ID
- Q96GD0
- Uniprot Name
- Pyridoxal phosphate phosphatase
- Molecular Weight
- 31697.735 Da
References
- Jang YM, Kim DW, Kang TC, Won MH, Baek NI, Moon BJ, Choi SY, Kwon OS: Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution. J Biol Chem. 2003 Dec 12;278(50):50040-6. Epub 2003 Sep 30. [Article]
- McCarty MF: Increased homocyst(e)ine associated with smoking, chronic inflammation, and aging may reflect acute-phase induction of pyridoxal phosphatase activity. Med Hypotheses. 2000 Oct;55(4):289-93. [Article]
- Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [Article]
- Kim DW, Eum WS, Choi HS, Kim SY, An JJ, Lee SH, Sohn EJ, Hwang SI, Kwon OS, Kang TC, Won MH, Cho SW, Lee KS, Park J, Choi SY: Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies. J Biochem Mol Biol. 2005 Nov 30;38(6):703-8. [Article]
- Tirrell IM, Wall JL, Daley CJ, Denial SJ, Tennis FG, Galens KG, O'Handley SF: YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily. Biochem J. 2006 Mar 15;394(Pt 3):665-74. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Serine c-palmitoyltransferase activity
- Specific Function
- Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the subst...
- Gene Name
- SPTLC1
- Uniprot ID
- O15269
- Uniprot Name
- Serine palmitoyltransferase 1
- Molecular Weight
- 52743.41 Da
References
- Hanada K: Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. [Article]
- Gable K, Han G, Monaghan E, Bacikova D, Natarajan M, Williams R, Dunn TM: Mutations in the yeast LCB1 and LCB2 genes, including those corresponding to the hereditary sensory neuropathy type I mutations, dominantly inactivate serine palmitoyltransferase. J Biol Chem. 2002 Mar 22;277(12):10194-200. Epub 2002 Jan 7. [Article]
- Ikushiro H, Hayashi H, Kagamiyama H: A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction. J Biol Chem. 2001 May 25;276(21):18249-56. Epub 2001 Mar 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two c...
- Gene Name
- CTH
- Uniprot ID
- P32929
- Uniprot Name
- Cystathionine gamma-lyase
- Molecular Weight
- 44507.64 Da
References
- Yamagata S, Akamatsu T, Iwama T: Immobilization of Saccharomyces cerevisiae cystathionine gamma-lyase and application of the product to cystathionine synthesis. Appl Environ Microbiol. 2004 Jun;70(6):3766-8. [Article]
- Bertoldi M, Cellini B, Laurents DV, Borri Voltattorni C: Folding pathway of the pyridoxal 5'-phosphate C-S lyase MalY from Escherichia coli. Biochem J. 2005 Aug 1;389(Pt 3):885-98. [Article]
- Lowicka E, Beltowski J: Hydrogen sulfide (H2S) - the third gas of interest for pharmacologists. Pharmacol Rep. 2007 Jan-Feb;59(1):4-24. [Article]
- Lima CP, Davis SR, Mackey AD, Scheer JB, Williamson J, Gregory JF 3rd: Vitamin B-6 deficiency suppresses the hepatic transsulfuration pathway but increases glutathione concentration in rats fed AIN-76A or AIN-93G diets. J Nutr. 2006 Aug;136(8):2141-7. [Article]
- Okuno T, Kubota T, Kuroda T, Ueno H, Nakamuro K: Contribution of enzymic alpha, gamma-elimination reaction in detoxification pathway of selenomethionine in mouse liver. Toxicol Appl Pharmacol. 2001 Oct 1;176(1):18-23. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- L-valine transaminase activity
- Specific Function
- Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine.
- Gene Name
- BCAT1
- Uniprot ID
- P54687
- Uniprot Name
- Branched-chain-amino-acid aminotransferase, cytosolic
- Molecular Weight
- 42965.815 Da
References
- Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- L-valine transaminase activity
- Specific Function
- Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids.
- Gene Name
- BCAT2
- Uniprot ID
- O15382
- Uniprot Name
- Branched-chain-amino-acid aminotransferase, mitochondrial
- Molecular Weight
- 44287.445 Da
References
- Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM: Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. Biochemistry. 2002 Oct 1;41(39):11592-601. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Binder
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- PROSC
- Uniprot ID
- O94903
- Uniprot Name
- Proline synthase co-transcribed bacterial homolog protein
- Molecular Weight
- 30343.7 Da
References
- Fux A, Sieber SA: Biochemical and Proteomic Studies of Human Pyridoxal 5'-Phosphate-Binding Protein (PLPBP). ACS Chem Biol. 2020 Jan 17;15(1):254-261. doi: 10.1021/acschembio.9b00857. Epub 2019 Dec 26. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange betwe...
- Gene Name
- GOT2
- Uniprot ID
- P00505
- Uniprot Name
- Aspartate aminotransferase, mitochondrial
- Molecular Weight
- 47517.285 Da
References
- Mavrides C, Orr W: Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J Biol Chem. 1975 Jun 10;250(11):4128-33. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
- Gene Name
- PYGB
- Uniprot ID
- P11216
- Uniprot Name
- Glycogen phosphorylase, brain form
- Molecular Weight
- 96695.18 Da
References
- Hudson JW, Hefferon KL, Crerar MM: Comparative analysis of species-independent, isozyme-specific amino-acid substitutions in mammalian muscle, brain and liver glycogen phosphorylases. Biochim Biophys Acta. 1993 Jul 10;1164(2):197-208. doi: 10.1016/0167-4838(93)90248-p. [Article]
- Hudson JW, Golding GB, Crerar MM: Evolution of allosteric control in glycogen phosphorylase. J Mol Biol. 1993 Dec 5;234(3):700-21. doi: 10.1006/jmbi.1993.1621. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known ...
- Gene Name
- PYGM
- Uniprot ID
- P11217
- Uniprot Name
- Glycogen phosphorylase, muscle form
- Molecular Weight
- 97091.265 Da
References
- Livanova NB, Chebotareva NA, Eronina TB, Kurganov BI: Pyridoxal 5'-phosphate as a catalytic and conformational cofactor of muscle glycogen phosphorylase B. Biochemistry (Mosc). 2002 Oct;67(10):1089-98. [Article]
- Kurganov BI, Kornilaev BA, Chebotareva NA, Malikov VP, Orlov VN, Lyubarev AE, Livanova NB: Dissociative mechanism of thermal denaturation of rabbit skeletal muscle glycogen phosphorylase b. Biochemistry. 2000 Oct 31;39(43):13144-52. [Article]
- Okada M, Shibuya M, Yamamoto E, Murakami Y: Effect of diabetes on vitamin B6 requirement in experimental animals. Diabetes Obes Metab. 1999 Jul;1(4):221-5. [Article]
- Okada M, Goda H, Kondo Y, Murakami Y, Shibuya M: Effect of exercise on the metabolism of vitamin B6 and some PLP-dependent enzymes in young rats fed a restricted vitamin B6 diet. J Nutr Sci Vitaminol (Tokyo). 2001 Apr;47(2):116-21. [Article]
- Geremia S, Campagnolo M, Schinzel R, Johnson LN: Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J Mol Biol. 2002 Sep 13;322(2):413-23. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine.
- Gene Name
- DDC
- Uniprot ID
- P20711
- Uniprot Name
- Aromatic-L-amino-acid decarboxylase
- Molecular Weight
- 53925.815 Da
References
- Rahman MK, Nagatsu T, Sakurai T, Hori S, Abe M, Matsuda M: Effect of pyridoxal phosphate deficiency on aromatic L-amino acid decarboxylase activity with L-DOPA and L-5-hydroxytryptophan as substrates in rats. Jpn J Pharmacol. 1982 Oct;32(5):803-11. [Article]
- Rorsman F, Husebye ES, Winqvist O, Bjork E, Karlsson FA, Kampe O: Aromatic-L-amino-acid decarboxylase, a pyridoxal phosphate-dependent enzyme, is a beta-cell autoantigen. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8626-9. [Article]
- Bertoldi M, Borri Voltattorni C: Reaction of dopa decarboxylase with L-aromatic amino acids under aerobic and anaerobic conditions. Biochem J. 2000 Dec 1;352 Pt 2:533-8. [Article]
- Allen GF, Neergheen V, Oppenheim M, Fitzgerald JC, Footitt E, Hyland K, Clayton PT, Land JM, Heales SJ: Pyridoxal 5'-phosphate deficiency causes a loss of aromatic L-amino acid decarboxylase in patients and human neuroblastoma cells, implications for aromatic L-amino acid decarboxylase and vitamin B(6) deficiency states. J Neurochem. 2010 Jul;114(1):87-96. doi: 10.1111/j.1471-4159.2010.06742.x. Epub 2010 Apr 9. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Interconversion of serine and glycine.
- Gene Name
- Not Available
- Uniprot ID
- Q53ET4
- Uniprot Name
- Serine hydroxymethyltransferase
- Molecular Weight
- 55973.345 Da
References
- Mehta R, Shangari N, O'Brien PJ: Preventing cell death induced by carbonyl stress, oxidative stress or mitochondrial toxins with vitamin B anti-AGE agents. Mol Nutr Food Res. 2008 Mar;52(3):379-85. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the production of GABA.
- Gene Name
- GAD2
- Uniprot ID
- Q05329
- Uniprot Name
- Glutamate decarboxylase 2
- Molecular Weight
- 65410.77 Da
References
- Cormier-Daire V, Dagoneau N, Nabbout R, Burglen L, Penet C, Soufflet C, Desguerre I, Munnich A, Dulac O: A gene for pyridoxine-dependent epilepsy maps to chromosome 5q31. Am J Hum Genet. 2000 Oct;67(4):991-3. Epub 2000 Sep 7. [Article]
- NIH gene review [Link]
- Genome JP reference [Link]
- Regulatory Properties of Brain Glutamate Decarboxylase (GAD): The Apoenzyme of GAD Is Present Principally as the Smaller of Two Molecular Forms of GAD in Brain [Link]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)c...
- Gene Name
- CCBL2
- Uniprot ID
- Q6YP21
- Uniprot Name
- Kynurenine--oxoglutarate transaminase 3
- Molecular Weight
- 51399.855 Da
References
- Nematollahi A, Sun G, Jayawickrama GS, Church WB: Kynurenine Aminotransferase Isozyme Inhibitors: A Review. Int J Mol Sci. 2016 Jun 15;17(6). pii: ijms17060946. doi: 10.3390/ijms17060946. [Article]
- Nematollahi A, Church WB, Nadvi NA, Gorrell MD, Sun G: Homology modeling of human kynurenine aminotransferase III and observations on inhibitor binding using molecular docking. Cent Nerv Syst Agents Med Chem. 2014;14(1):2-9. doi: 10.2174/1871524914666140416095523. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Sulfinoalanine decarboxylase activity
- Specific Function
- May catalyze the decarboxylation of aspartate, cysteine sulfinic acid, and cysteic acid to beta-alanine, hypotaurine and taurine, respectively. Does not exhibit any decarboxylation activity toward ...
- Gene Name
- GADL1
- Uniprot ID
- Q6ZQY3
- Uniprot Name
- Acidic amino acid decarboxylase GADL1
- Molecular Weight
- 59245.95 Da
References
- Liu P, Ge X, Ding H, Jiang H, Christensen BM, Li J: Role of glutamate decarboxylase-like protein 1 (GADL1) in taurine biosynthesis. J Biol Chem. 2012 Nov 30;287(49):40898-906. doi: 10.1074/jbc.M112.393728. Epub 2012 Oct 4. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Transferase activity
- Specific Function
- Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium.
- Gene Name
- SCLY
- Uniprot ID
- Q96I15
- Uniprot Name
- Selenocysteine lyase
- Molecular Weight
- 48148.45 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Not Available
- Specific Function
- May be involved in the maintenance of osteochondroprogenitor cells pool.
- Gene Name
- IGSF10
- Uniprot ID
- Q6WRI0
- Uniprot Name
- Immunoglobulin superfamily member 10
- Molecular Weight
- 290835.42 Da
References
- Berman HM, Westbrook J, Feng Z, Gilliland G, Bhat TN, Weissig H, Shindyalov IN, Bourne PE: The Protein Data Bank. Nucleic Acids Res. 2000 Jan 1;28(1):235-42. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Transaminase activity
- Specific Function
- Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde.
- Gene Name
- PHYKPL
- Uniprot ID
- Q8IUZ5
- Uniprot Name
- 5-phosphohydroxy-L-lysine phospho-lyase
- Molecular Weight
- 49710.245 Da
References
- Veiga-da-Cunha M, Hadi F, Balligand T, Stroobant V, Van Schaftingen E: Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine. J Biol Chem. 2012 Mar 2;287(10):7246-55. doi: 10.1074/jbc.M111.323485. Epub 2012 Jan 12. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.
- Gene Name
- SHMT2
- Uniprot ID
- P34897
- Uniprot Name
- Serine hydroxymethyltransferase, mitochondrial
- Molecular Weight
- 55992.385 Da
References
- Bhavani S, Trivedi V, Jala VR, Subramanya HS, Kaul P, Prakash V, Appaji Rao N, Savithri HS: Role of Lys-226 in the catalytic mechanism of Bacillus stearothermophilus serine hydroxymethyltransferase--crystal structure and kinetic studies. Biochemistry. 2005 May 10;44(18):6929-37. [Article]
- Trivedi V, Gupta A, Jala VR, Saravanan P, Rao GS, Rao NA, Savithri HS, Subramanya HS: Crystal structure of binary and ternary complexes of serine hydroxymethyltransferase from Bacillus stearothermophilus: insights into the catalytic mechanism. J Biol Chem. 2002 May 10;277(19):17161-9. Epub 2002 Feb 27. [Article]
- Perry C, Yu S, Chen J, Matharu KS, Stover PJ: Effect of vitamin B6 availability on serine hydroxymethyltransferase in MCF-7 cells. Arch Biochem Biophys. 2007 Jun 1;462(1):21-7. Epub 2007 Apr 20. [Article]
- Rajaram V, Bhavani BS, Kaul P, Prakash V, Appaji Rao N, Savithri HS, Murthy MR: Structure determination and biochemical studies on Bacillus stearothermophilus E53Q serine hydroxymethyltransferase and its complexes provide insights on function and enzyme memory. FEBS J. 2007 Aug;274(16):4148-60. Epub 2007 Jul 25. [Article]
- Mukherjee M, Sievers SA, Brown MT, Johnson PJ: Identification and biochemical characterization of serine hydroxymethyl transferase in the hydrogenosome of Trichomonas vaginalis. Eukaryot Cell. 2006 Dec;5(12):2072-8. Epub 2006 Sep 15. [Article]
- Trakatellis A, Dimitriadou A, Exindari M, Christodoulou D, Malissiovas N, Antoniadis A, Haitoglou K: Effect of combination of deoxypyridoxine with known anti-proliferative or immunosuppressive agents on lymphocyte serine hydroxymethyltransferase. Postgrad Med J. 1994;70 Suppl 1:S89-92. [Article]
- Jagath JR, Sharma B, Rao NA, Savithri HS: The role of His-134, -147, and -150 residues in subunit assembly, cofactor binding, and catalysis of sheep liver cytosolic serine hydroxymethyltransferase. J Biol Chem. 1997 Sep 26;272(39):24355-62. [Article]
- Bourguignon J, Neuburger M, Douce R: Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase. Biochem J. 1988 Oct 1;255(1):169-78. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- ALAS2
- Uniprot ID
- P22557
- Uniprot Name
- 5-aminolevulinate synthase, erythroid-specific, mitochondrial
- Molecular Weight
- 64632.86 Da
References
- Shoolingin-Jordan PM, Al-Daihan S, Alexeev D, Baxter RL, Bottomley SS, Kahari ID, Roy I, Sarwar M, Sawyer L, Wang SF: 5-Aminolevulinic acid synthase: mechanism, mutations and medicine. Biochim Biophys Acta. 2003 Apr 11;1647(1-2):361-6. [Article]
- Choi HP, Hong JW, Rhee KH, Sung HC: Cloning, expression, and characterization of 5-aminolevulinic acid synthase from Rhodopseudomonas palustris KUGB306. FEMS Microbiol Lett. 2004 Jul 15;236(2):175-81. [Article]
- Heller T, Hochstetter V, Basler M, Borck V: [Vitamin B6-sensitive hereditary sideroblastic anemia]. Dtsch Med Wochenschr. 2004 Jan 23;129(4):141-4. [Article]
- Clayton PT: B6-responsive disorders: a model of vitamin dependency. J Inherit Metab Dis. 2006 Apr-Jun;29(2-3):317-26. [Article]
- Astner I, Schulze JO, van den Heuvel J, Jahn D, Schubert WD, Heinz DW: Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans. EMBO J. 2005 Sep 21;24(18):3166-77. Epub 2005 Aug 25. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate.
- Gene Name
- GPT2
- Uniprot ID
- Q8TD30
- Uniprot Name
- Alanine aminotransferase 2
- Molecular Weight
- 57903.11 Da
References
- Welch S: Comparative studies on the human glutamate-pyruvate transaminase phenotypes--GPT 1, GPT 2-1, GPT 2. Humangenetik. 1975 Sep 20;30(3):237-49. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Transferase activity
- Specific Function
- Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and...
- Gene Name
- MOCOS
- Uniprot ID
- Q96EN8
- Uniprot Name
- Molybdenum cofactor sulfurase
- Molecular Weight
- 98118.965 Da
References
- Heidenreich T, Wollers S, Mendel RR, Bittner F: Characterization of the NifS-like domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration. J Biol Chem. 2005 Feb 11;280(6):4213-8. Epub 2004 Nov 22. [Article]
- Mendel RR, Bittner F: Cell biology of molybdenum. Biochim Biophys Acta. 2006 Jul;1763(7):621-35. Epub 2006 May 12. [Article]
- Anantharaman V, Aravind L: MOSC domains: ancient, predicted sulfur-carrier domains, present in diverse metal-sulfur cluster biosynthesis proteins including Molybdenum cofactor sulfurases. FEMS Microbiol Lett. 2002 Jan 22;207(1):55-61. [Article]
- Bittner F, Oreb M, Mendel RR: ABA3 is a molybdenum cofactor sulfurase required for activation of aldehyde oxidase and xanthine dehydrogenase in Arabidopsis thaliana. J Biol Chem. 2001 Nov 2;276(44):40381-4. Epub 2001 Sep 11. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Has low serine dehydratase and threonine dehydratase activity.
- Gene Name
- SDSL
- Uniprot ID
- Q96GA7
- Uniprot Name
- Serine dehydratase-like
- Molecular Weight
- 34674.01 Da
References
- Yamada T, Komoto J, Kasuya T, Takata Y, Ogawa H, Mori H, Takusagawa F: A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies. Biochim Biophys Acta. 2008 May;1780(5):809-18. doi: 10.1016/j.bbagen.2008.01.020. Epub 2008 Feb 19. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Threonine racemase activity
- Specific Function
- Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
- Gene Name
- SRR
- Uniprot ID
- Q9GZT4
- Uniprot Name
- Serine racemase
- Molecular Weight
- 36565.905 Da
References
- Hashimoto A, Yoshikawa M: Effect of aminooxyacetic acid on extracellular level of D-serine in rat striatum: an in vivo microdialysis study. Eur J Pharmacol. 2005 Nov 21;525(1-3):91-3. Epub 2005 Nov 14. [Article]
- Strisovsky K, Jiraskova J, Mikulova A, Rulisek L, Konvalinka J: Dual substrate and reaction specificity in mouse serine racemase: identification of high-affinity dicarboxylate substrate and inhibitors and analysis of the beta-eliminase activity. Biochemistry. 2005 Oct 4;44(39):13091-100. [Article]
- Schell MJ: The N-methyl D-aspartate receptor glycine site and D-serine metabolism: an evolutionary perspective. Philos Trans R Soc Lond B Biol Sci. 2004 Jun 29;359(1446):943-64. [Article]
- Strisovsky K, Jiraskova J, Barinka C, Majer P, Rojas C, Slusher BS, Konvalinka J: Mouse brain serine racemase catalyzes specific elimination of L-serine to pyruvate. FEBS Lett. 2003 Jan 30;535(1-3):44-8. [Article]
- Uo T, Yoshimura T, Nishiyama T, Esaki N: Gene cloning, purification, and characterization of 2,3-diaminopropionate ammonia-lyase from Escherichia coli. Biosci Biotechnol Biochem. 2002 Dec;66(12):2639-44. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Trna binding
- Specific Function
- Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
- Gene Name
- SEPSECS
- Uniprot ID
- Q9HD40
- Uniprot Name
- O-phosphoseryl-tRNA(Sec) selenium transferase
- Molecular Weight
- 55725.69 Da
References
- Xu XM, Carlson BA, Mix H, Zhang Y, Saira K, Glass RS, Berry MJ, Gladyshev VN, Hatfield DL: Biosynthesis of selenocysteine on its tRNA in eukaryotes. PLoS Biol. 2007 Jan;5(1):e4. [Article]
- Kernebeck T, Lohse AW, Grotzinger J: A bioinformatical approach suggests the function of the autoimmune hepatitis target antigen soluble liver antigen/liver pancreas. Hepatology. 2001 Aug;34(2):230-3. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Serine c-palmitoyltransferase activity
- Specific Function
- Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate ...
- Gene Name
- SPTLC3
- Uniprot ID
- Q9NUV7
- Uniprot Name
- Serine palmitoyltransferase 3
- Molecular Weight
- 62049.035 Da
References
- Lowther J, Naismith JH, Dunn TM, Campopiano DJ: Structural, mechanistic and regulatory studies of serine palmitoyltransferase. Biochem Soc Trans. 2012 Jun 1;40(3):547-54. doi: 10.1042/BST20110769. [Article]
- Hanada K: Serine palmitoyltransferase, a key enzyme of sphingolipid metabolism. Biochim Biophys Acta. 2003 Jun 10;1632(1-3):16-30. [Article]
- Hornemann T, Penno A, Rutti MF, Ernst D, Kivrak-Pfiffner F, Rohrer L, von Eckardstein A: The SPTLC3 subunit of serine palmitoyltransferase generates short chain sphingoid bases. J Biol Chem. 2009 Sep 25;284(39):26322-30. doi: 10.1074/jbc.M109.023192. Epub 2009 Aug 1. [Article]
- Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. doi: 10.1073/pnas.0811269106. Epub 2009 May 5. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Not Available
- Gene Name
- GAD65
- Uniprot ID
- Q9UGI5
- Uniprot Name
- Glutamic acid decarboxylase
- Molecular Weight
- 47343.69 Da
References
- Tong JC, Myers MA, Mackay IR, Zimmet PZ, Rowley MJ: The PEVKEK region of the pyridoxal phosphate binding domain of GAD65 expresses a dominant B cell epitope for type 1 diabetes sera. Ann N Y Acad Sci. 2002 Apr;958:182-9. [Article]
- Burd L, Stenehjem A, Franceschini LA, Kerbeshian J: A 15-year follow-up of a boy with pyridoxine (vitamin B6)-dependent seizures with autism, breath holding, and severe mental retardation. J Child Neurol. 2000 Nov;15(11):763-5. [Article]
- Myers MA, Davies JM, Tong JC, Whisstock J, Scealy M, Mackay IR, Rowley MJ: Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modeling. J Immunol. 2000 Oct 1;165(7):3830-8. [Article]
- Gospe SM Jr: Pyridoxine-dependent seizures: new genetic and biochemical clues to help with diagnosis and treatment. Curr Opin Neurol. 2006 Apr;19(2):148-53. [Article]
- Hwang IK, Yoo KY, Kim do H, Lee BH, Kwon YG, Won MH: Time course of changes in pyridoxal 5'-phosphate (vitamin B6 active form) and its neuroprotection in experimental ischemic damage. Exp Neurol. 2007 Jul;206(1):114-25. Epub 2007 Apr 24. [Article]
- Kind
- Protein group
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Cofactor
- General Function
- Pyridoxal phosphate binding
- Specific Function
- Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a sca...
Components:
| Name | UniProt ID |
|---|---|
| Aspartate aminotransferase, cytoplasmic | P17174 |
| Aspartate aminotransferase, mitochondrial | P00505 |
References
- Dajnowicz S, Parks JM, Hu X, Gesler K, Kovalevsky AY, Mueser TC: Direct evidence that an extended hydrogen-bonding network influences activation of pyridoxal 5'-phosphate in aspartate aminotransferase. J Biol Chem. 2017 Apr 7;292(14):5970-5980. doi: 10.1074/jbc.M116.774588. Epub 2017 Feb 23. [Article]
- Mueser TC, Drago V, Kovalevsky A, Dajnowicz S: Pyridoxal 5'-phosphate dependent reactions: Analyzing the mechanism of aspartate aminotransferase. Methods Enzymol. 2020;634:333-359. doi: 10.1016/bs.mie.2020.01.009. Epub 2020 Feb 13. [Article]
- Rej R, Vanderlinde RE: Effects of buffers on aspartate aminotransferase activity and association of the enzyme with pyridoxal phosphate. Clin Chem. 1975 Oct;21(11):1585-91. [Article]
Drug created at June 13, 2005 13:24 / Updated at February 13, 2024 02:57