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Decarboxylases C
Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).
Overview
The decarboxylases generate CO2 and the indicated products from acidic substrates, requiring pyridoxal phosphate or pyruvic acid as a co-factor.
Enzymes
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GAD1 (Glutamic acid decarboxylase 1) C Show summary »« Hide summary
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GAD2 (Glutamic acid decarboxylase 2) C Show summary »« Hide summary
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HDC (Histidine decarboxylase) C Show summary »« Hide summary
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ADC (L-Arginine decarboxylase ) C Show summary »« Hide summary
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AADC (L-Aromatic amino-acid decarboxylase )
C
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MLYCD (Malonyl-CoA decarboxylase)
C
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ODC (Ornithine decarboxylase)
C
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PSDC (Phosphatidylserine decarboxylase ) C Show summary »« Hide summary
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SAMDC (S-Adenosylmethionine decarboxylase ) C Show summary »« Hide summary
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References
1. Coleman CS, Hu G, Pegg AE. (2004) Putrescine biosynthesis in mammalian tissues. Biochem. J., 379 (Pt 3): 849-55. [PMID:14763899]
2. Daidone F, Montioli R, Paiardini A, Cellini B, Macchiarulo A, Giardina G, Bossa F, Borri Voltattorni C. (2012) Identification by virtual screening and in vitro testing of human DOPA decarboxylase inhibitors. PLoS ONE, 7 (2): e31610. [PMID:22384042]
3. Garbarg M, Barbin G, Rodergas E, Schwartz JC. (1980) Inhibition of histamine synthesis in brain by alpha-fluoromethylhistidine, a new irreversible inhibitor: in vitro and in vivo studies. J. Neurochem., 35 (5): 1045-52. [PMID:7452304]
4. Malmlöf T, Feltmann K, Konradsson-Geuken Å, Schneider F, Alken RG, Svensson TH, Schilström B. (2015) Deuterium-substituted L-DOPA displays increased behavioral potency and dopamine output in an animal model of Parkinson's disease: comparison with the effects produced by L-DOPA and an MAO-B inhibitor. J Neural Transm, 122 (2): 259-72. [PMID:24906468]
5. Pajunen AE, Hietala OA, Baruch-Virransalo EL, Piha RS. (1979) The effect of DL-allylglycine on polyamine and GABA metabolism in mouse brain. J. Neurochem., 32 (5): 1401-8. [PMID:438812]
6. Qu N, Ignatenko NA, Yamauchi P, Stringer DE, Levenson C, Shannon P, Perrin S, Gerner EW. (2003) Inhibition of human ornithine decarboxylase activity by enantiomers of difluoromethylornithine. Biochem. J., 375 (Pt 2): 465-70. [PMID:12859253]
7. Saha AK, Schwarsin AJ, Roduit R, Masse F, Kaushik V, Tornheim K, Prentki M, Ruderman NB. (2000) Activation of malonyl-CoA decarboxylase in rat skeletal muscle by contraction and the AMP-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-beta -D-ribofuranoside. J. Biol. Chem., 275 (32): 24279-83. [PMID:10854420]
8. Stanek J, Caravatti G, Frei J, Furet P, Mett H, Schneider P, Regenass U. (1993) 4-Amidinoindan-1-one 2'-amidinohydrazone: a new potent and selective inhibitor of S-Adenosylmethionine decarboxylase. J. Med. Chem., 36 (15): 2168-71. [PMID:8340919]
9. Stanek J, Frei J, Mett H, Schneider P, Regenass U. (1992) 2-substituted 3-(aminooxy)propanamines as inhibitors of ornithine decarboxylase: synthesis and biological activity. J. Med. Chem., 35 (8): 1339-44. [PMID:1573631]
10. Tang H, Yan Y, Feng Z, de Jesus RK, Yang L, Levorse DA, Owens KA, Akiyama TE, Bergeron R, Castriota GA et al.. (2010) Design and synthesis of a new class of malonyl-CoA decarboxylase inhibitors with anti-obesity and anti-diabetic activities. Bioorg. Med. Chem. Lett., 20 (20): 6088-92. [PMID:20832306]
11. Wu JY, Matsuda T, Roberts E. (1973) Purification and characterization of glutamate decarboxylase from mouse brain. J. Biol. Chem., 248 (9): 3029-34. [PMID:4700449]
12. Zhu MY, Iyo A, Piletz JE, Regunathan S. (2004) Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine. Biochim. Biophys. Acta, 1670 (2): 156-64. [PMID:14738999]
How to cite this family page
Database page citation:
Decarboxylases. Accessed on 12/07/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=256.
Concise Guide to PHARMACOLOGY citation:
Alexander SPH, Fabbro D, Kelly E, Marrion N, Peters JA, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Southan C, Davies JA and CGTP Collaborators (2015) The Concise Guide to PHARMACOLOGY 2015/16: Enzymes. Br J Pharmacol. 172: 6024-6109.
