Identification
- Generic Name
- Spermine
- DrugBank Accession Number
- DB00127
- Background
Spermine is a spermidine-derived biogenic polyamine found as a polycation at all pH values. Found in various tissues and organisms, it often acts as an essential growth factor in some bacterial species. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure.
- Type
- Small Molecule
- Groups
- Experimental, Nutraceutical
- Structure
Structure for Spermine (DB00127)
- Weight
- Average: 202.3402
Monoisotopic: 202.215746852 - Chemical Formula
- C10H26N4
- Synonyms
- 4,9-diaza-1,12-dodecanediamine
- 4,9-diazadodecane-1,12-diamine
- Musculamine
- N,N'-Bis(3-aminopropyl)-1,4-butanediamine
- Spermina
- Spermine
- External IDs
- NSC-268508
Pharmacology
- Indication
For nutritional supplementation, also for treating dietary shortage or imbalance
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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
Spermine is a polyamine. It is an organic molecule that is involved in cellular metabolism.
- Mechanism of action
Spermine is derived from spermidine by spermine synthase. Spermine is a polyamine, a small organic cations that is absolutely required for eukaryotic cell growth. Spermine, is normally found in millimolar concentrations in the nucleus. Spermine functions directly as a free radical scavenger, and forms a variety of adducts that prevent oxidative damage to DNA. Oxidative damage to DNA by reactive oxygen species is a continual problem that cells must guard against to survive. Hence, spermine is a major natural intracellular compound capable of protecting DNA from free radical attack. Spermine is also implicated in the regulation of gene expression, the stabilization of chromatin, and the prevention of endonuclease-mediated DNA fragmentation.
Target Actions Organism ASpermine synthase ligandHumans ASpermine oxidase ligandHumans ADNA binderHumans UOrnithine decarboxylase product ofHumans UExtracellular calcium-sensing receptor Not Available Humans UBeta-1 adrenergic receptor Not Available Humans UBeta-2 adrenergic receptor Not Available Humans - 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
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Not Available
- Pathways
Pathway Category Spermidine and Spermine Biosynthesis Metabolic - 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.
Drug Interaction Integrate drug-drug
interactions in your softwareAcyclovir The risk or severity of adverse effects can be increased when Acyclovir is combined with Spermine. Amantadine The risk or severity of adverse effects can be increased when Amantadine is combined with Spermine. Chlorpheniramine The risk or severity of adverse effects can be increased when Chlorpheniramine is combined with Spermine. Choline The risk or severity of adverse effects can be increased when Choline is combined with Spermine. Choline salicylate The risk or severity of adverse effects can be increased when Choline salicylate is combined with Spermine. - Food Interactions
- Not Available
Products
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Ingredient UNII CAS InChI Key Spermine dihydrate Not Available 403982-64-9 MTNRSMVAYLLBAV-UHFFFAOYSA-N
Categories
- Drug Categories
- Chemical TaxonomyProvided by Classyfire
- Description
- This compound belongs to the class of organic compounds known as dialkylamines. These are organic compounds containing a dialkylamine group, characterized by two alkyl groups bonded to the amino nitrogen.
- Kingdom
- Organic compounds
- Super Class
- Organic nitrogen compounds
- Class
- Organonitrogen compounds
- Sub Class
- Amines
- Direct Parent
- Dialkylamines
- Alternative Parents
- Organopnictogen compounds / Monoalkylamines / Hydrocarbon derivatives
- Substituents
- Aliphatic acyclic compound / Hydrocarbon derivative / Organopnictogen compound / Primary aliphatic amine / Primary amine / Secondary aliphatic amine
- Molecular Framework
- Aliphatic acyclic compounds
- External Descriptors
- tetraamine, polyazaalkane (CHEBI:15746)
- Affected organisms
- Humans and other mammals
Chemical Identifiers
- UNII
- 2FZ7Y3VOQX
- CAS number
- 71-44-3
- InChI Key
- PFNFFQXMRSDOHW-UHFFFAOYSA-N
- InChI
- InChI=1S/C10H26N4/c11-5-3-9-13-7-1-2-8-14-10-4-6-12/h13-14H,1-12H2
- IUPAC Name
- (3-aminopropyl)({4-[(3-aminopropyl)amino]butyl})amine
- SMILES
- NCCCNCCCCNCCCN
References
- Synthesis Reference
Koji Nakanishi, Amira T. Eldefrawi, Mohyee E. Eldefrawi, Peter N. R. Usherwood, "Butyryl-tyrosinyl spermine, analogs thereof and methods of preparing and using same." U.S. Patent US5770625, issued January, 1966.
US5770625- General References
- Not Available
- External Links
- Human Metabolome Database
- HMDB0001256
- KEGG Compound
- C00750
- PubChem Compound
- 1103
- PubChem Substance
- 46507215
- ChemSpider
- 1072
- BindingDB
- 79403
- 1483263
- ChEBI
- 15746
- ChEMBL
- CHEMBL23194
- ZINC
- ZINC000001532734
- PharmGKB
- PA164781199
- Guide to Pharmacology
- GtP Drug Page
- PDBe Ligand
- SPM
- Wikipedia
- Spermine
- PDB Entries
- 100d / 131d / 198d / 1d10 / 1d12 / 1d15 / 1d48 / 1dcr / 1dns / 1dpl … show 189 more
- MSDS
- Download (19.4 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 0 Completed Prevention NEC / Premature Births 1
Pharmacoeconomics
- Manufacturers
- Not Available
- Packagers
- Not Available
- Dosage Forms
- Not Available
- Prices
- Not Available
- Patents
- Not Available
Properties
- State
- Solid
- Experimental Properties
Property Value Source melting point (°C) 29 °C PhysProp boiling point (°C) 150-150 °C Not Available water solubility > 100 mg/mL Not Available logP -0.7 Not Available - Predicted Properties
Property Value Source Water Solubility 2.19 mg/mL ALOGPS logP -0.66 ALOGPS logP -1.5 Chemaxon logS -2 ALOGPS pKa (Strongest Basic) 10.8 Chemaxon Physiological Charge 4 Chemaxon Hydrogen Acceptor Count 4 Chemaxon Hydrogen Donor Count 4 Chemaxon Polar Surface Area 76.1 Å2 Chemaxon Rotatable Bond Count 11 Chemaxon Refractivity 62.56 m3·mol-1 Chemaxon Polarizability 26.69 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 + 0.9215 Blood Brain Barrier + 0.6345 Caco-2 permeable + 0.7072 P-glycoprotein substrate Non-substrate 0.5094 P-glycoprotein inhibitor I Non-inhibitor 0.9178 P-glycoprotein inhibitor II Non-inhibitor 0.6414 Renal organic cation transporter Non-inhibitor 0.6066 CYP450 2C9 substrate Non-substrate 0.8863 CYP450 2D6 substrate Non-substrate 0.5607 CYP450 3A4 substrate Non-substrate 0.8262 CYP450 1A2 substrate Inhibitor 0.877 CYP450 2C9 inhibitor Non-inhibitor 0.9072 CYP450 2D6 inhibitor Non-inhibitor 0.9502 CYP450 2C19 inhibitor Non-inhibitor 0.9026 CYP450 3A4 inhibitor Non-inhibitor 0.9703 CYP450 inhibitory promiscuity Low CYP Inhibitory Promiscuity 0.9386 Ames test Non AMES toxic 0.8957 Carcinogenicity Non-carcinogens 0.6436 Biodegradation Ready biodegradable 0.5525 Rat acute toxicity 2.4561 LD50, mol/kg Not applicable hERG inhibition (predictor I) Weak inhibitor 0.7691 hERG inhibition (predictor II) Non-inhibitor 0.7739
Spectra
- Mass Spec (NIST)
- Download (10.5 KB)
- Spectra
- Chromatographic Properties
Collision Cross Sections (CCS)
Adduct CCS Value (Å2) Source type Source [M-H]- 157.0870987 predictedDarkChem Lite v0.1.0 [M-H]- 157.2835987 predictedDarkChem Lite v0.1.0 [M-H]- 145.28842 predictedDeepCCS 1.0 (2019) [M+H]+ 157.5024987 predictedDarkChem Lite v0.1.0 [M+H]+ 156.9285987 predictedDarkChem Lite v0.1.0 [M+H]+ 148.63876 predictedDeepCCS 1.0 (2019) [M+Na]+ 157.2674987 predictedDarkChem Lite v0.1.0 [M+Na]+ 157.6892987 predictedDarkChem Lite v0.1.0 [M+Na]+ 158.01805 predictedDeepCCS 1.0 (2019)
Targets
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- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Ligand
- General Function
- Spermine synthase activity
- Specific Function
- Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
- Gene Name
- SMS
- Uniprot ID
- P52788
- Uniprot Name
- Spermine synthase
- Molecular Weight
- 41267.855 Da
References
- Lopatin AN, Shantz LM, Mackintosh CA, Nichols CG, Pegg AE: Modulation of potassium channels in the hearts of transgenic and mutant mice with altered polyamine biosynthesis. J Mol Cell Cardiol. 2000 Nov;32(11):2007-24. [Article]
- Korhonen VP, Niiranen K, Halmekyto M, Pietila M, Diegelman P, Parkkinen JJ, Eloranta T, Porter CW, Alhonen L, Janne J: Spermine deficiency resulting from targeted disruption of the spermine synthase gene in embryonic stem cells leads to enhanced sensitivity to antiproliferative drugs. Mol Pharmacol. 2001 Feb;59(2):231-8. [Article]
- Cason AL, Ikeguchi Y, Skinner C, Wood TC, Holden KR, Lubs HA, Martinez F, Simensen RJ, Stevenson RE, Pegg AE, Schwartz CE: X-linked spermine synthase gene (SMS) defect: the first polyamine deficiency syndrome. Eur J Hum Genet. 2003 Dec;11(12):937-44. [Article]
- Wang X, Ikeguchi Y, McCloskey DE, Nelson P, Pegg AE: Spermine synthesis is required for normal viability, growth, and fertility in the mouse. J Biol Chem. 2004 Dec 3;279(49):51370-5. Epub 2004 Sep 30. [Article]
- Schwartz CE, Wang X, Stevenson RE, Pegg AE: Spermine synthase deficiency resulting in X-linked intellectual disability (Snyder-Robinson syndrome). Methods Mol Biol. 2011;720:437-45. doi: 10.1007/978-1-61779-034-8_28. [Article]
- Wang X, Pegg AE: Use of (Gyro) Gy and spermine synthase transgenic mice to study functions of spermine. Methods Mol Biol. 2011;720:159-70. doi: 10.1007/978-1-61779-034-8_9. [Article]
- Theiss C, Bohley P, Voigt J: Regulation by polyamines of ornithine decarboxylase activity and cell division in the unicellular green alga Chlamydomonas reinhardtii. Plant Physiol. 2002 Apr;128(4):1470-9. [Article]
- Krauss M, Langnaese K, Richter K, Brunk I, Wieske M, Ahnert-Hilger G, Veh RW, Laube G: Spermidine synthase is prominently expressed in the striatal patch compartment and in putative interneurones of the matrix compartment. J Neurochem. 2006 Apr;97(1):174-89. Epub 2006 Mar 3. [Article]
- Kobayashi M, Takao K, Shiota Y, Sugita Y, Takahashi M, Nakae D, Samejima K: Inhibition of putrescine aminopropyltransferase influences rat liver regeneration. Biol Pharm Bull. 2006 May;29(5):863-7. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Yes
- Actions
- Ligand
- General Function
- Spermine:oxygen oxidoreductase (spermidine-forming) activity
- Specific Function
- Flavoenzyme which catalyzes the oxidation of spermine to spermidine. Can also use N(1)-acetylspermine and spermidine as substrates, with different affinity depending on the isoform (isozyme) and on...
- Gene Name
- SMOX
- Uniprot ID
- Q9NWM0
- Uniprot Name
- Spermine oxidase
- Molecular Weight
- 61818.76 Da
References
- Binda C, Angelini R, Federico R, Ascenzi P, Mattevi A: Structural bases for inhibitor binding and catalysis in polyamine oxidase. Biochemistry. 2001 Mar 6;40(9):2766-76. [Article]
- Vujcic S, Diegelman P, Bacchi CJ, Kramer DL, Porter CW: Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell origin. Biochem J. 2002 Nov 1;367(Pt 3):665-75. [Article]
- Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem J. 2003 Feb 15;370(Pt 1):19-28. [Article]
- Wang Y, Murray-Stewart T, Devereux W, Hacker A, Frydman B, Woster PM, Casero RA Jr: Properties of purified recombinant human polyamine oxidase, PAOh1/SMO. Biochem Biophys Res Commun. 2003 May 16;304(4):605-11. [Article]
- Bacchi CJ, Rattendi D, Faciane E, Yarlett N, Weiss LM, Frydman B, Woster P, Wei B, Marton LJ, Wittner M: Polyamine metabolism in a member of the phylum Microspora (Encephalitozoon cuniculi): effects of polyamine analogues. Microbiology. 2004 May;150(Pt 5):1215-24. [Article]
Yes
Binder
References
- Trubetskoy VS, Wolff JA, Budker VG: The role of a microscopic colloidally stabilized phase in solubilizing oligoamine-condensed DNA complexes. Biophys J. 2003 Feb;84(2 Pt 1):1124-30. [Article]
- Cho SK, Kwon YJ: Polyamine/DNA polyplexes with acid-degradable polymeric shell as structurally and functionally virus-mimicking nonviral vectors. J Control Release. 2011 Mar 30;150(3):287-97. doi: 10.1016/j.jconrel.2010.12.004. Epub 2010 Dec 16. [Article]
- Saminathan M, Thomas T, Shirahata A, Pillai CK, Thomas TJ: Polyamine structural effects on the induction and stabilization of liquid crystalline DNA: potential applications to DNA packaging, gene therapy and polyamine therapeutics. Nucleic Acids Res. 2002 Sep 1;30(17):3722-31. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Product of
- 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
- Nilsson J, Grahn B, Heby O: Antizyme inhibitor is rapidly induced in growth-stimulated mouse fibroblasts and releases ornithine decarboxylase from antizyme suppression. Biochem J. 2000 Mar 15;346 Pt 3:699-704. [Article]
- Ray RM, Viar MJ, Yuan Q, Johnson LR: Polyamine depletion delays apoptosis of rat intestinal epithelial cells. Am J Physiol Cell Physiol. 2000 Mar;278(3):C480-9. [Article]
- Korhonen VP, Niiranen K, Halmekyto M, Pietila M, Diegelman P, Parkkinen JJ, Eloranta T, Porter CW, Alhonen L, Janne J: Spermine deficiency resulting from targeted disruption of the spermine synthase gene in embryonic stem cells leads to enhanced sensitivity to antiproliferative drugs. Mol Pharmacol. 2001 Feb;59(2):231-8. [Article]
- Rohn G, Els T, Hell K, Ernestus RI: Regional distribution of ornithine decarboxylase activity and polyamine levels in experimental cat brain tumors. Neurochem Int. 2001 Aug;39(2):135-40. [Article]
- Ernestus RI, Rohn G, Schroder R, Els T, Klekner A, Paschen W, Klug N: Polyamine metabolism in brain tumours: diagnostic relevance of quantitative biochemistry. J Neurol Neurosurg Psychiatry. 2001 Jul;71(1):88-92. [Article]
- Lee NK, MacLean HE: Polyamines, androgens, and skeletal muscle hypertrophy. J Cell Physiol. 2011 Jun;226(6):1453-60. doi: 10.1002/jcp.22569. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Phosphatidylinositol phospholipase c activity
- Specific Function
- Senses changes in the extracellular concentration of calcium ions. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system.
- Gene Name
- CASR
- Uniprot ID
- P41180
- Uniprot Name
- Extracellular calcium-sensing receptor
- Molecular Weight
- 120672.385 Da
References
- El Hiani Y, Ahidouch A, Roudbaraki M, Guenin S, Brule G, Ouadid-Ahidouch H: Calcium-sensing receptor stimulation induces nonselective cation channel activation in breast cancer cells. J Membr Biol. 2006;211(2):127-37. Epub 2006 Oct 14. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Receptor signaling protein activity
- Specific Function
- Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately e...
- Gene Name
- ADRB1
- Uniprot ID
- P08588
- Uniprot Name
- Beta-1 adrenergic receptor
- Molecular Weight
- 51322.1 Da
References
- Meana C, Bordallo J, Bordallo C, Suarez L, Cantabrana B, Sanchez M: Functional effects of polyamines via activation of human beta1- and beta2-adrenoceptors stably expressed in CHO cells. Pharmacol Rep. 2010 Jul-Aug;62(4):696-706. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- General Function
- Protein homodimerization activity
- Specific Function
- Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately ...
- Gene Name
- ADRB2
- Uniprot ID
- P07550
- Uniprot Name
- Beta-2 adrenergic receptor
- Molecular Weight
- 46458.32 Da
References
- Meana C, Bordallo J, Bordallo C, Suarez L, Cantabrana B, Sanchez M: Functional effects of polyamines via activation of human beta1- and beta2-adrenoceptors stably expressed in CHO cells. Pharmacol Rep. 2010 Jul-Aug;62(4):696-706. [Article]
Enzymes
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Diamine n-acetyltransferase activity
- Specific Function
- Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine at...
- Gene Name
- SAT1
- Uniprot ID
- P21673
- Uniprot Name
- Diamine acetyltransferase 1
- Molecular Weight
- 20023.8 Da
References
- Vujcic S, Halmekyto M, Diegelman P, Gan G, Kramer DL, Janne J, Porter CW: Effects of conditional overexpression of spermidine/spermine N1-acetyltransferase on polyamine pool dynamics, cell growth, and sensitivity to polyamine analogs. J Biol Chem. 2000 Dec 8;275(49):38319-28. [Article]
- Hegardt C, Andersson G, Oredsson SM: Changes in polyamine metabolism during glucocorticoid-induced programmed cell death in mouse thymus. Cell Biol Int. 2000;24(12):871-80. [Article]
- Marverti G, Bettuzzi S, Astancolle S, Pinna C, Monti MG, Moruzzi MS: Differential induction of spermidine/spermine N1-acetyltransferase activity in cisplatin-sensitive and -resistant ovarian cancer cells in response to N1,N12-bis(ethyl)spermine involves transcriptional and post-transcriptional regulation. Eur J Cancer. 2001 Jan;37(2):281-9. [Article]
- Scorcioni F, Corti A, Davalli P, Astancolle S, Bettuzzi S: Manipulation of the expression of regulatory genes of polyamine metabolism results in specific alterations of the cell-cycle progression. Biochem J. 2001 Feb 15;354(Pt 1):217-23. [Article]
- Min SH, Simmen RC, Alhonen L, Halmekyto M, Porter CW, Janne J, Simmen FA: Altered levels of growth-related and novel gene transcripts in reproductive and other tissues of female mice overexpressing spermidine/spermine N1-acetyltransferase (SSAT). J Biol Chem. 2002 Feb 1;277(5):3647-57. Epub 2001 Nov 14. [Article]
- Limsuwun K, Jones PG: Spermidine acetyltransferase is required to prevent spermidine toxicity at low temperatures in Escherichia coli. J Bacteriol. 2000 Oct;182(19):5373-80. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Diamine n-acetyltransferase activity
- Specific Function
- Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N(1)acetylspermine = putrescine.
- Gene Name
- SAT2
- Uniprot ID
- Q96F10
- Uniprot Name
- Diamine acetyltransferase 2
- Molecular Weight
- 19154.905 Da
References
- Chen Y, Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of a second spermidine/spermine N1-acetyltransferase. Biochem J. 2003 Aug 1;373(Pt 3):661-7. [Article]
- Coleman CS, Stanley BA, Jones AD, Pegg AE: Spermidine/spermine-N1-acetyltransferase-2 (SSAT2) acetylates thialysine and is not involved in polyamine metabolism. Biochem J. 2004 Nov 15;384(Pt 1):139-48. [Article]
- Vogel NL, Boeke M, Ashburner BP: Spermidine/Spermine N1-Acetyltransferase 2 (SSAT2) functions as a coactivator for NF-kappaB and cooperates with CBP and P/CAF to enhance NF-kappaB-dependent transcription. Biochim Biophys Acta. 2006 Oct;1759(10):470-7. Epub 2006 Aug 30. [Article]
- Limsuwun K, Jones PG: Spermidine acetyltransferase is required to prevent spermidine toxicity at low temperatures in Escherichia coli. J Bacteriol. 2000 Oct;182(19):5373-80. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Xanthine oxidase activity
- Specific Function
- Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Ha...
- Gene Name
- XDH
- Uniprot ID
- P47989
- Uniprot Name
- Xanthine dehydrogenase/oxidase
- Molecular Weight
- 146422.99 Da
References
- Lovaas E, Carlin G: Spermine: an anti-oxidant and anti-inflammatory agent. Free Radic Biol Med. 1991;11(5):455-61. [Article]
Transporters
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Inhibitor
- General Function
- Symporter activity
- Specific Function
- Sodium-ion dependent, low affinity carnitine transporter. Probably transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without...
- Gene Name
- SLC22A4
- Uniprot ID
- Q9H015
- Uniprot Name
- Solute carrier family 22 member 4
- Molecular Weight
- 62154.48 Da
References
- Yabuuchi H, Tamai I, Nezu J, Sakamoto K, Oku A, Shimane M, Sai Y, Tsuji A: Novel membrane transporter OCTN1 mediates multispecific, bidirectional, and pH-dependent transport of organic cations. J Pharmacol Exp Ther. 1999 May;289(2):768-73. [Article]
- Kind
- Protein
- Organism
- Humans
- Pharmacological action
- Unknown
- Actions
- Substrate
- General Function
- Secondary active organic cation transmembrane transporter activity
- Specific Function
- Translocates a broad array of organic cations with various structures and molecular weights including the model compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-methylnico...
- Gene Name
- SLC22A1
- Uniprot ID
- O15245
- Uniprot Name
- Solute carrier family 22 member 1
- Molecular Weight
- 61153.345 Da
References
- Busch AE, Quester S, Ulzheimer JC, Waldegger S, Gorboulev V, Arndt P, Lang F, Koepsell H: Electrogenic properties and substrate specificity of the polyspecific rat cation transporter rOCT1. J Biol Chem. 1996 Dec 20;271(51):32599-604. [Article]
- Li DC, Nichols CG, Sala-Rabanal M: Role of a Hydrophobic Pocket in Polyamine Interactions with the Polyspecific Organic Cation Transporter OCT3. J Biol Chem. 2015 Nov 13;290(46):27633-43. doi: 10.1074/jbc.M115.668913. Epub 2015 Sep 24. [Article]
Drug created at June 13, 2005 13:24 / Updated at January 02, 2024 23:42