Identification
- Summary
Ornithine is an amino acid commonly found as a component in total parenteral nutrition.
- Brand Names
- Primene
- Generic Name
- Ornithine
- DrugBank Accession Number
- DB00129
- Background
Produced during the urea cycle, ornithine is an amino acid produced from the splitting off of urea from arginine. L-Ornithine allows for the disposal of excess nitrogen and acts as a precursor of citrulline and arginine.
- Type
- Small Molecule
- Groups
- Approved, Nutraceutical
- Structure
Structure for Ornithine (DB00129)
- Weight
- Average: 132.161
Monoisotopic: 132.089877638 - Chemical Formula
- C5H12N2O2
- Synonyms
- (S)-2,5-Diaminopentanoate
- (S)-2,5-Diaminopentanoic acid
- (S)-2,5-diaminovaleric acid
- (S)-ornithine
- (S)-α,δ-diaminovaleric acid
- L-Ornithine
- levo-ornithine
- Ornithine
- Ornithinum
- Ornitina
Pharmacology
- Indication
Used for nutritional supplementation, also for treating dietary shortage or imbalance. It has been claimed that ornithine improves athletic performance, has anabolic effects, has wound-healing effects, and is immuno-enhancing.
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Indication Type Indication Combined Product Details Approval Level Age Group Patient Characteristics Dose Form Treatment of Hepatic encephalopathy (he) •••••••••••• •••••••• •••••••••• •••••••• - 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
A non-essential and nonprotein amino acid, ornithine is critical for the production of the body's proteins, enzymes and muscle tissue. Ornithine plays a central role in the urea cycle and is important for the disposal of excess nitrogen (ammonia). Ornithine is the starting point for the synthesis of many polyamines such as putrescine and spermine. Ornithine supplements are claimed to enhance the release of growth hormone and to burn excess body fat. Ornithine is necessary for proper immune function and good liver function.
- Mechanism of action
L-Ornithine is metabolised to L-arginine. L-arginine stimulates the pituitary release of growth hormone. Burns or other injuries affect the state of L-arginine in tissues throughout the body. As De novo synthesis of L-arginine during these conditions is usually not sufficient for normal immune function, nor for normal protein synthesis, L-ornithine may have immunomodulatory and wound-healing activities under these conditions (by virtue of its metabolism to L-arginine).
Target Actions Organism UOrnithine aminotransferase, mitochondrial Not Available Humans UOrnithine carbamoyltransferase, mitochondrial Not Available Humans UArginase-1 Not Available Humans UOrnithine decarboxylase antizyme 1 Not Available Humans UHigh affinity cationic amino acid transporter 1 Not Available Humans ULow affinity cationic amino acid transporter 2 Not Available Humans UMitochondrial ornithine transporter 2 Not Available Humans UArginase-2, mitochondrial Not Available Humans UMitochondrial ornithine transporter 1 Not Available Humans UGlycine amidinotransferase, mitochondrial Not Available Humans - Absorption
Absorbed from the small intestine via a sodium-dependent active transport process
- Volume of distribution
Not Available
- Protein binding
Not Available
- Metabolism
Ornithine undergoes extensive metabolism in the liver to L-arginine, polyamines, and proline, and several other metabolites.
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- Route of elimination
Not Available
- Half-life
Not Available
- Clearance
Not Available
- Adverse Effects
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Oral, rat LD50 = 10000 mg/kg
- Pathways
- Pharmacogenomic Effects/ADRs Browse all" title="About SNP Mediated Effects/ADRs" id="snp-actions-info" class="drug-info-popup" href="javascript:void(0);">
- Not Available
Interactions
- Drug Interactions Learn More" title="About Drug Interactions" id="structured-interactions-info" class="drug-info-popup" href="javascript:void(0);">
- 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 Ornithine aspartate JA08T3B97O 3230-94-2 IXUZXIMQZIMPSQ-ZBRNBAAYSA-N Ornithine dihydrochloride 8N284L2VLC 6211-16-1 HGBAVEGDXFHRQP-FHNDMYTFSA-N Ornithine hydrochloride HBK84K66XH 3184-13-2 GGTYBZJRPHEQDG-WCCKRBBISA-N Ornithine oxoglurate 4FEN49K96W 5191-97-9 SLPUVFBNQHVEEU-WCCKRBBISA-N - Mixture Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image AMINOPLASMAL-10% E INFUSION Ornithine hydrochloride (2.51 g/l) + Acetylcysteine (0.5 g/l) + Alanine (13.7 g/l) + Arginine (9.2 g/l) + Asparagine (3.27 g/l) + Aspartic acid (1.3 g/l) + Glutamic acid (4.6 g/l) + Glycine (7.9 g/l) + Histidine (5.2 g/l) + Isoleucine (5.1 g/l) + Leucine (8.9 g/l) + Lysine hydrochloride (5.6 g/l) + Magnesium acetate (0.56 g/l) + Malic acid (1.01 g/l) + Methionine (3.8 g/l) + N-acetyltyrosine (1 g/l) + Phenylalanine (5.1 g/l) + Potassium acetate (2.45 g/l) + Proline (8.9 g/l) + Serine (2.4 g/l) + Sodium acetate (3.95 g/l) + Sodium hydroxide (0.2 g/l) + Sodium phosphate, monobasic (1.4 g/l) + Threonine (4.1 g/l) + Tryptophan (1.8 g/l) + Tyrosine (0.3 g/l) + Valine (4.8 g/l) Injection Intravenous B. BRAUN SINGAPORE PTE LTD 1991-05-13 Not applicable Singapore 
AMINOPLASMAL-5% E INFUSION Ornithine hydrochloride (1.25 g/1000ml) + Acetylcysteine (0.25 g/1000ml) + Alanine (6.85 g/1000ml) + Arginine (4.6 g/1000ml) + Asparagine (1.64 g/1000ml) + Aspartic acid (0.65 g/1000ml) + Glutamic acid (2.3 g/1000ml) + Glycine (3.95 g/1000ml) + Histidine (2.6 g/1000ml) + Isoleucine (2.55 g/1000ml) + Leucine (4.45 g/1000ml) + Lysine hydrochloride (2.8 g/1000ml) + Magnesium acetate (0.56 g/1000ml) + Malic acid (1.01 g/1000ml) + Methionine (1.9 g/1000ml) + N-acetyltyrosine (0.35 g/1000ml) + Phenylalanine (2.55 g/1000ml) + Potassium acetate (2.45 g/1000ml) + Proline (4.45 g/1000ml) + Serine (1.2 g/1000ml) + Sodium acetate (3.95 g/1000ml) + Sodium hydroxide (0.2 g/1000ml) + Sodium phosphate, monobasic (1.4 g/1000ml) + Threonine (2.05 g/1000ml) + Tryptophan (0.9 g/1000ml) + Tyrosine (0.3 g/1000ml) + Valine (2.4 g/1000ml) Injection Intravenous B. BRAUN SINGAPORE PTE LTD 1991-05-13 Not applicable Singapore NUMETA Ornithine (0.23 g/300ml) + Alanine (0.75 g/300ml) + Arginine (0.78 g/300ml) + Aspartic acid (0.56 g/300ml) + Calcium chloride dihydrate (0.55 g/300ml) + Cysteine (0.18 g/300ml) + D-glucose (40 g/300ml) + Glutamic acid (0.93 g/300ml) + Glycine (0.37 g/300ml) + Histidine (0.35 g/300ml) + Isoleucine (0.62 g/300ml) + Leucine (0.93 g/300ml) + Lysine (1.03 g/300ml) + Magnesium acetate tetrahydrate (0.1 g/300ml) + Methionine (0.22 g/300ml) + Olive oil (6 g/300ml) + Phenylalanine (0.39 g/300ml) + Potassium acetate (0.61 g/300ml) + Proline (0.28 g/300ml) + Serine (0.37 g/300ml) + Sodium glycerophosphate hydrate (0.98 g/300ml) + Soybean oil (1.5 g/300ml) + Taurine (0.06 g/300ml) + Threonine (0.35 g/300ml) + Tryptophan (0.19 g/300ml) + Tyrosine (0.07 g/300ml) + Valine (0.71 g/300ml) Injection, emulsion Parenteral Baxter S.P.A. 2016-10-15 Not applicable Italy 
Numeta G 13 % E Emulsion zur Infusion Ornithine hydrochloride (1.45 g) + Alanine (4.66 g) + Arginine (4.89 g) + Aspartic acid (3.5 g) + Calcium chloride dihydrate (3.45 g) + Cysteine (1.1 g) + D-glucose monohydrate (550 g) + Glutamic acid (5.83 g) + Glycine (2.33 g) + Histidine (2.21 g) + Isoleucine (3.9 g) + Leucine (5.83 g) + Lysine monohydrate (6.41 g) + Magnesium acetate tetrahydrate (0.63 g) + Methionine (1.4 g) + Olive oil (6 g) + Phenylalanine (2.45 g) + Potassium acetate (3.83 g) + Proline (1.75 g) + Serine (2.33 g) + Sodium glycerophosphate hydrate (6.15 g) + Soybean oil (1.5 g) + Taurine (0.35 g) + Threonine (2.16 g) + Tryptophan (1.17 g) + Tyrosine (0.45 g) + Valine (4.43 g) Injection, emulsion Parenteral Baxter Healthcare Gmb H 2016-05-11 Not applicable Austria 
Numeta G 16 % E Emulsion zur Infusion Ornithine hydrochloride (0.41 g) + Alanine (1.03 g) + Arginine (1.08 g) + Aspartic acid (0.77 g) + Calcium chloride dihydrate (0.46 g) + Cysteine (0.24 g) + D-glucose monohydrate (85.25 g) + Glutamic acid (1.29 g) + Glycine (0.51 g) + Histidine (0.49 g) + Isoleucine (0.86 g) + Leucine (1.29 g) + Lysine monohydrate (1.59 g) + Magnesium acetate tetrahydrate (0.33 g) + Methionine (0.31 g) + Olive oil (12.4 g) + Phenylalanine (0.54 g) + Potassium acetate (1.12 g) + Proline (0.39 g) + Serine (0.51 g) + Sodium chloride (0.3 g) + Sodium glycerophosphate hydrate (0.98 g) + Soybean oil (3.1 g) + Taurine (0.08 g) + Threonine (0.48 g) + Tryptophan (0.26 g) + Tyrosine (0.1 g) + Valine (0.98 g) Injection, emulsion Intravenous Baxter Healthcare Gmb H 2011-03-17 Not applicable Austria - Unapproved/Other Products
Name Ingredients Dosage Route Labeller Marketing Start Marketing End Region Image Primene Ornithine hydrochloride (0.8 g/250mL) + Alanine (2 g/250mL) + Arginine (2.1 g/250mL) + Aspartic acid (1.5 g/250mL) + Cysteine (0.47 g/250mL) + Glutamic acid (2.5 g/250mL) + Glycine (1 g/250mL) + Histidine (0.95 g/250mL) + Isoleucine (1.675 g/250mL) + Leucine (2.5 g/250mL) + Lysine (2.75 g/250mL) + Methionine (0.6 g/250mL) + Phenylalanine (1.05 g/250mL) + Proline (0.75 g/250mL) + Serine (1 g/250mL) + Taurine (0.15 g/250mL) + Threonine (0.9 g/250mL) + Tryptophan (0.5 g/250mL) + Tyrosine (0.11 g/250mL) + Valine (1.9 g/250mL) Injection, solution Intravenous Baxter Healthcare Corporation 2017-11-22 2019-05-31 US 
Categories
- ATC Codes
- A05BA06 — Ornithine oxoglurate
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as l-alpha-amino acids. These are alpha amino acids which have the L-configuration of the alpha-carbon atom.
- Kingdom
- Organic compounds
- Super Class
- Organic acids and derivatives
- Class
- Carboxylic acids and derivatives
- Sub Class
- Amino acids, peptides, and analogues
- Direct Parent
- L-alpha-amino acids
- Alternative Parents
- Fatty acids and conjugates / Amino acids / Monocarboxylic acids and derivatives / Carboxylic acids / Organopnictogen compounds / Organic oxides / Monoalkylamines / Hydrocarbon derivatives / Carbonyl compounds
- Substituents
- Aliphatic acyclic compound / Amine / Amino acid / Carbonyl group / Carboxylic acid / Fatty acid / Hydrocarbon derivative / L-alpha-amino acid / Monocarboxylic acid or derivatives / Organic nitrogen compound
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- non-proteinogenic L-alpha-amino acid, ornithine (CHEBI:15729) / Other amino acids (C00077)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- E524N2IXA3
- CAS number
- 70-26-8
- InChI Key
- AHLPHDHHMVZTML-BYPYZUCNSA-N
- InChI
- InChI=1S/C5H12N2O2/c6-3-1-2-4(7)5(8)9/h4H,1-3,6-7H2,(H,8,9)/t4-/m0/s1
- IUPAC Name
- (2S)-2,5-diaminopentanoic acid
- SMILES
- NCCC[C@H](N)C(O)=O
References
- Synthesis Reference
Takayasu Tsuchida, Haruo Uchibori, Yoshitaka Nishimoto, "Process and microorganism for producing L-ornithine by Corynebacterium, Brevibacterium, or Athrobacter." U.S. Patent US5188947, issued January, 1970.
US5188947- General References
- External Links
- Human Metabolome Database
- HMDB0000214
- KEGG Compound
- C00077
- PubChem Compound
- 6262
- PubChem Substance
- 46505239
- ChemSpider
- 6026
- BindingDB
- 50487430
- 7704
- ChEBI
- 15729
- ChEMBL
- CHEMBL446143
- ZINC
- ZINC000001532530
- PharmGKB
- PA164783814
- Guide to Pharmacology
- GtP Drug Page
- PDBe Ligand
- ORN
- PDRhealth
- PDRhealth Drug Page
- Wikipedia
- Ornithine
- PDB Entries
- 1a9x / 1b2h / 1bxr / 1c30 / 1c3o / 1ce8 / 1cs0 / 1hqg / 1hth / 1jdb … show 137 more
- MSDS
- Download (72.9 KB)
Clinical Trials
- Clinical Trials Learn More" title="About Clinical Trials" id="clinical-trials-info" class="drug-info-popup" href="javascript:void(0);">
Phase Status Purpose Conditions Count 4 Completed Prevention Hepatic Encephalopathy (HE) 1 4 Completed Treatment Cirrhosis of the Liver / Hepatic Encephalopathy (HE) 1 4 Completed Treatment Hepatic Encephalopathy (HE) 2 4 Not Yet Recruiting Treatment Hepatic Encephalopathy Stage 2 / Hepatic Encephalopathy Stage 3 / Hepatic Encephalopathy Stage 4 1 4 Recruiting Treatment Cirrhosis of the Liver 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
Form Route Strength Injection Intravenous 0.5 g/l Injection Intravenous 0.25 g/1000ml Tablet Oral Granule Oral 3 g Granule, for solution Oral Solution, concentrate Intravenous 5 g Granule Intravenous Granule Intravenous 3 g Solution Intravenous drip 5 g Granule Intravenous 5 g Granule, for solution Oral 3 g Injection, solution, concentrate Intravenous 5 g/10ml Granule, effervescent Oral 5 g Injection, solution Intravenous 5 g/10mL Granule Oral Injection Intravenous Injection, emulsion Parenteral Injection, emulsion Intravenous Emulsion Intravenous Emulsion Intravenous 0.466 g Powder Intravenous Solution Parenteral Injection, solution Intravenous Solution Intravenous Injection Intravenous Injection Intravenous 4 g/l Liquid Intravenous Solution - Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 140 °C PhysProp water solubility Appreciable Not Available logP -4.22 SANGSTER (1994) pKa 1.94 (at 25 °C) KORTUM,G ET AL (1961) - Predicted Properties
Property Value Source Water Solubility 172.0 mg/mL ALOGPS logP -3.6 ALOGPS logP -3.7 Chemaxon logS 0.11 ALOGPS pKa (Strongest Acidic) 2.67 Chemaxon pKa (Strongest Basic) 10.29 Chemaxon Physiological Charge 1 Chemaxon Hydrogen Acceptor Count 4 Chemaxon Hydrogen Donor Count 3 Chemaxon Polar Surface Area 89.34 Å2 Chemaxon Rotatable Bond Count 4 Chemaxon Refractivity 33.21 m3·mol-1 Chemaxon Polarizability 13.85 Å3 Chemaxon Number of Rings 0 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 + 0.8449 Blood Brain Barrier + 0.7613 Caco-2 permeable - 0.7431 P-glycoprotein substrate Non-substrate 0.6568 P-glycoprotein inhibitor I Non-inhibitor 0.9856 P-glycoprotein inhibitor II Non-inhibitor 0.9681 Renal organic cation transporter Non-inhibitor 0.8847 CYP450 2C9 substrate Non-substrate 0.8464 CYP450 2D6 substrate Non-substrate 0.7517 CYP450 3A4 substrate Non-substrate 0.8238 CYP450 1A2 substrate Non-inhibitor 0.9653 CYP450 2C9 inhibitor Non-inhibitor 0.9639 CYP450 2D6 inhibitor Non-inhibitor 0.9786 CYP450 2C19 inhibitor Non-inhibitor 0.9659 CYP450 3A4 inhibitor Non-inhibitor 0.9327 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9931 Ames test AMES toxic 0.8541 Carcinogenicity Non-carcinogens 0.8407 Biodegradation Ready biodegradable 0.8711 Rat acute toxicity 1.0540 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.9771 hERG inhibition (predictor II) Non-inhibitor 0.9663
Spectra
- Mass Spec (NIST)
- Not Available
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 129.034942 predictedDarkChem Lite v0.1.0 [M-H]- 126.3708153 predictedDarkChem Standard v0.1.0 [M-H]- 128.909542 predictedDarkChem Lite v0.1.0 [M-H]- 123.595 predictedDeepCCS 1.0 (2019) [M+H]+ 129.273642 predictedDarkChem Lite v0.1.0 [M+H]+ 126.8479442 predictedDarkChem Standard v0.1.0 [M+H]+ 129.473742 predictedDarkChem Lite v0.1.0 [M+H]+ 126.750946 predictedDeepCCS 1.0 (2019) [M+Na]+ 128.910442 predictedDarkChem Lite v0.1.0 [M+Na]+ 128.891742 predictedDarkChem Lite v0.1.0 [M+Na]+ 129.136042 predictedDarkChem Lite v0.1.0 [M+Na]+ 135.44458 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- 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
- Levillain O, Balvay S, Peyrol S: Localization and differential expression of arginase II in the kidney of male and female mice. Pflugers Arch. 2005 Feb;449(5):491-503. Epub 2004 Dec 23. [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]
- Kaneko S, Ueda-Yamada M, Ando A, Matsumura S, Okuda-Ashitaka E, Matsumura M, Uyama M, Ito S: Cytotoxic effect of spermine on retinal pigment epithelial cells. Invest Ophthalmol Vis Sci. 2007 Jan;48(1):455-63. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Phospholipid binding
- Specific Function
- Not Available
- Gene Name
- OTC
- Uniprot ID
- P00480
- Uniprot Name
- Ornithine carbamoyltransferase, mitochondrial
- Molecular Weight
- 39934.775 Da
References
- Barcelona-Andres B, Marina A, Rubio V: Gene structure, organization, expression, and potential regulatory mechanisms of arginine catabolism in Enterococcus faecalis. J Bacteriol. 2002 Nov;184(22):6289-300. [Article]
- El Alami M, Dubois E, Oudjama Y, Tricot C, Wouters J, Stalon V, Messenguy F: Yeast epiarginase regulation, an enzyme-enzyme activity control: identification of residues of ornithine carbamoyltransferase and arginase responsible for enzyme catalytic and regulatory activities. J Biol Chem. 2003 Jun 13;278(24):21550-8. Epub 2003 Apr 4. [Article]
- Templeton MD, Reinhardt LA, Collyer CA, Mitchell RE, Cleland WW: Kinetic analysis of the L-ornithine transcarbamoylase from Pseudomonas savastanoi pv. phaseolicola that is resistant to the transition state analogue (R)-N delta-(N'-sulfodiaminophosphinyl)-L-ornithine. Biochemistry. 2005 Mar 22;44(11):4408-15. [Article]
- Morizono H, Cabrera-Luque J, Shi D, Gallegos R, Yamaguchi S, Yu X, Allewell NM, Malamy MH, Tuchman M: Acetylornithine transcarbamylase: a novel enzyme in arginine biosynthesis. J Bacteriol. 2006 Apr;188(8):2974-82. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Manganese ion binding
- Specific Function
- Not Available
- Gene Name
- ARG1
- Uniprot ID
- P05089
- Uniprot Name
- Arginase-1
- Molecular Weight
- 34734.655 Da
References
- Gobert AP, Cheng Y, Wang JY, Boucher JL, Iyer RK, Cederbaum SD, Casero RA Jr, Newton JC, Wilson KT: Helicobacter pylori induces macrophage apoptosis by activation of arginase II. J Immunol. 2002 May 1;168(9):4692-700. [Article]
- Iwata S, Tsujino T, Ikeda Y, Ishida T, Ueyama T, Gotoh T, Mori M, Yokoyama M: Decreased expression of arginase II in the kidneys of Dahl salt-sensitive rats. Hypertens Res. 2002 May;25(3):411-8. [Article]
- Stickings P, Mistry SK, Boucher JL, Morris SM, Cunningham JM: Arginase expression and modulation of IL-1beta-induced nitric oxide generation in rat and human islets of Langerhans. Nitric Oxide. 2002 Dec;7(4):289-96. [Article]
- Bansal V, Ochoa JB: Arginine availability, arginase, and the immune response. Curr Opin Clin Nutr Metab Care. 2003 Mar;6(2):223-8. [Article]
- El Alami M, Dubois E, Oudjama Y, Tricot C, Wouters J, Stalon V, Messenguy F: Yeast epiarginase regulation, an enzyme-enzyme activity control: identification of residues of ornithine carbamoyltransferase and arginase responsible for enzyme catalytic and regulatory activities. J Biol Chem. 2003 Jun 13;278(24):21550-8. Epub 2003 Apr 4. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Ornithine decarboxylase inhibitor activity
- Specific Function
- Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake by binding to and targeting ODC1 for degradation (PubMed:17...
- Gene Name
- OAZ1
- Uniprot ID
- P54368
- Uniprot Name
- Ornithine decarboxylase antizyme 1
- Molecular Weight
- 25405.265 Da
References
- Lopez-Contreras AJ, Lopez-Garcia C, Jimenez-Cervantes C, Cremades A, Penafiel R: Mouse ornithine decarboxylase-like gene encodes an antizyme inhibitor devoid of ornithine and arginine decarboxylating activity. J Biol Chem. 2006 Oct 13;281(41):30896-906. Epub 2006 Aug 17. [Article]
- Yamaguchi Y, Takatsuka Y, Matsufuji S, Murakami Y, Kamio Y: Characterization of a counterpart to Mammalian ornithine decarboxylase antizyme in prokaryotes. J Biol Chem. 2006 Feb 17;281(7):3995-4001. Epub 2005 Dec 14. [Article]
- Janne J, Alhonen L, Pietila M, Keinanen TA: Genetic approaches to the cellular functions of polyamines in mammals. Eur J Biochem. 2004 Mar;271(5):877-94. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- L-ornithine transmembrane transporter activity
- Specific Function
- High-affinity, low capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine) in non-hepatic tissues. May also function as an ecotropic retroviral leuk...
- Gene Name
- SLC7A1
- Uniprot ID
- P30825
- Uniprot Name
- High affinity cationic amino acid transporter 1
- Molecular Weight
- 67637.62 Da
References
- Rotmann A, Strand D, Martine U, Closs EI: Protein kinase C activation promotes the internalization of the human cationic amino acid transporter hCAT-1. A new regulatory mechanism for hCAT-1 activity. J Biol Chem. 2004 Dec 24;279(52):54185-92. Epub 2004 Oct 15. [Article]
- Cerec V, Piquet-Pellorce C, Aly HA, Touzalin AM, Jegou B, Bauche F: Multiple pathways for cationic amino acid transport in rat seminiferous tubule cells. Biol Reprod. 2007 Feb;76(2):241-9. Epub 2006 Oct 25. [Article]
- Yeramian A, Martin L, Arpa L, Bertran J, Soler C, McLeod C, Modolell M, Palacin M, Lloberas J, Celada A: Macrophages require distinct arginine catabolism and transport systems for proliferation and for activation. Eur J Immunol. 2006 Jun;36(6):1516-26. [Article]
- Kaneko S, Ando A, Okuda-Ashitaka E, Maeda M, Furuta K, Suzuki M, Matsumura M, Ito S: Ornithine transport via cationic amino acid transporter-1 is involved in ornithine cytotoxicity in retinal pigment epithelial cells. Invest Ophthalmol Vis Sci. 2007 Jan;48(1):464-71. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Low-affinity l-arginine transmembrane transporter activity
- Specific Function
- Functions as permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine); the affinity for its substrates differs between isoforms created by alternative splicin...
- Gene Name
- SLC7A2
- Uniprot ID
- P52569
- Uniprot Name
- Cationic amino acid transporter 2
- Molecular Weight
- 71672.175 Da
References
- Yeramian A, Martin L, Arpa L, Bertran J, Soler C, McLeod C, Modolell M, Palacin M, Lloberas J, Celada A: Macrophages require distinct arginine catabolism and transport systems for proliferation and for activation. Eur J Immunol. 2006 Jun;36(6):1516-26. [Article]
- Cerec V, Piquet-Pellorce C, Aly HA, Touzalin AM, Jegou B, Bauche F: Multiple pathways for cationic amino acid transport in rat seminiferous tubule cells. Biol Reprod. 2007 Feb;76(2):241-9. Epub 2006 Oct 25. [Article]
- Endo M, Oyadomari S, Terasaki Y, Takeya M, Suga M, Mori M, Gotoh T: Induction of arginase I and II in bleomycin-induced fibrosis of mouse lung. Am J Physiol Lung Cell Mol Physiol. 2003 Aug;285(2):L313-21. Epub 2003 Apr 4. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Not Available
- Specific Function
- Ornithine transport across inner mitochondrial membrane, from the cytoplasm to the matrix.
- Gene Name
- SLC25A2
- Uniprot ID
- Q9BXI2
- Uniprot Name
- Mitochondrial ornithine transporter 2
- Molecular Weight
- 32580.07 Da
References
- Camacho JA, Rioseco-Camacho N, Andrade D, Porter J, Kong J: Cloning and characterization of human ORNT2: a second mitochondrial ornithine transporter that can rescue a defective ORNT1 in patients with the hyperornithinemia-hyperammonemia-homocitrullinuria syndrome, a urea cycle disorder. Mol Genet Metab. 2003 Aug;79(4):257-71. [Article]
- Begum L, Jalil MA, Kobayashi K, Iijima M, Li MX, Yasuda T, Horiuchi M, del Arco A, Satrustegui J, Saheki T: Expression of three mitochondrial solute carriers, citrin, aralar1 and ornithine transporter, in relation to urea cycle in mice. Biochim Biophys Acta. 2002 Apr 12;1574(3):283-92. [Article]
- Camacho JA, Mardach R, Rioseco-Camacho N, Ruiz-Pesini E, Derbeneva O, Andrade D, Zaldivar F, Qu Y, Cederbaum SD: Clinical and functional characterization of a human ORNT1 mutation (T32R) in the hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome. Pediatr Res. 2006 Oct;60(4):423-9. Epub 2006 Aug 28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Metal ion binding
- Specific Function
- May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailabili...
- Gene Name
- ARG2
- Uniprot ID
- P78540
- Uniprot Name
- Arginase-2, mitochondrial
- Molecular Weight
- 38577.515 Da
References
- Rodriguez PC, Zea AH, DeSalvo J, Culotta KS, Zabaleta J, Quiceno DG, Ochoa JB, Ochoa AC: L-arginine consumption by macrophages modulates the expression of CD3 zeta chain in T lymphocytes. J Immunol. 2003 Aug 1;171(3):1232-9. [Article]
- Levillain O, Hus-Citharel A, Garvi S, Peyrol S, Reymond I, Mutin M, Morel F: Ornithine metabolism in male and female rat kidney: mitochondrial expression of ornithine aminotransferase and arginase II. Am J Physiol Renal Physiol. 2004 Apr;286(4):F727-38. Epub 2004 Feb 10. [Article]
- Levillain O, Diaz JJ, Blanchard O, Dechaud H: Testosterone down-regulates ornithine aminotransferase gene and up-regulates arginase II and ornithine decarboxylase genes for polyamines synthesis in the murine kidney. Endocrinology. 2005 Feb;146(2):950-9. Epub 2004 Nov 11. [Article]
- Bussiere FI, Chaturvedi R, Cheng Y, Gobert AP, Asim M, Blumberg DR, Xu H, Kim PY, Hacker A, Casero RA Jr, Wilson KT: Spermine causes loss of innate immune response to Helicobacter pylori by inhibition of inducible nitric-oxide synthase translation. J Biol Chem. 2005 Jan 28;280(4):2409-12. Epub 2004 Nov 17. [Article]
- Nissim I, Luhovyy B, Horyn O, Daikhin Y, Nissim I, Yudkoff M: The role of mitochondrially bound arginase in the regulation of urea synthesis: studies with [U-15N4]arginine, isolated mitochondria, and perfused rat liver. J Biol Chem. 2005 May 6;280(18):17715-24. Epub 2005 Mar 7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- L-ornithine transmembrane transporter activity
- Specific Function
- Ornithine transport across inner mitochondrial membrane, from the cytoplasm to the matrix.
- Gene Name
- SLC25A15
- Uniprot ID
- Q9Y619
- Uniprot Name
- Mitochondrial ornithine transporter 1
- Molecular Weight
- 32735.96 Da
References
- Korman SH, Kanazawa N, Abu-Libdeh B, Gutman A, Tsujino S: Hyperornithinemia, hyperammonemia, and homocitrullinuria syndrome with evidence of mitochondrial dysfunction due to a novel SLC25A15 (ORNT1) gene mutation in a Palestinian family. J Neurol Sci. 2004 Mar 15;218(1-2):53-8. [Article]
- Camacho JA, Mardach R, Rioseco-Camacho N, Ruiz-Pesini E, Derbeneva O, Andrade D, Zaldivar F, Qu Y, Cederbaum SD: Clinical and functional characterization of a human ORNT1 mutation (T32R) in the hyperornithinemia-hyperammonemia-homocitrullinuria (HHH) syndrome. Pediatr Res. 2006 Oct;60(4):423-9. Epub 2006 Aug 28. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Glycine amidinotransferase activity
- Specific Function
- Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central ner...
- Gene Name
- GATM
- Uniprot ID
- P50440
- Uniprot Name
- Glycine amidinotransferase, mitochondrial
- Molecular Weight
- 48455.01 Da
References
- Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [Article]
- Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [Article]
- Thomasset N, Quash GA, Dore JF: The differential contribution of arginase and transamidinase to ornithine biosynthesis in two achromic human melanoma cell lines. FEBS Lett. 1982 Nov 1;148(1):63-6. [Article]
- Natesan S, Reddy SR: Compensatory changes in enzymes of arginine metabolism during renal hypertrophy in mice. Comp Biochem Physiol B Biochem Mol Biol. 2001 Dec;130(4):585-95. [Article]
- Mitruka BM, Costilow RN: Arginine and ornithine catabolism by Clostridium botulinum. J Bacteriol. 1967 Jan;93(1):295-301. [Article]
Drug created at June 13, 2005 13:24 / Updated at January 02, 2024 23:42