B6db activities : 4_1_1

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	4.1.1.19
Description	Arginine decarboxylase
Catalyzed reaction	L-arginine = agmatine + CO(2).
Cofactor	Pyridoxal-phosphate or pyruvate.
	Plant and proteobacterial (family 1) biosynthetic arginine decarboxylases are fold-type III enzymes. The Escherichia coli biodegradative arginine decarboxylase , other bacterial arginine decarboxylases (family 2) belong to the fold-type I group. In vertebrates, the production of agmatine may be accomplished by ornithine decarboxylase (EC 4.1.1.17). Mammalian paralogs of ornithine decarboxylase (fold-type III) were at one time attributed an arginine decarboxylase function, but subsequent studies proved that these proteins are not enzymes, but ornithine decarboxylase antizyme inhibitors (see ODCp). In archaea such as M. jannaschii, arginine decarboxylase is pyruvoyl-dependent.
Prosite	PROSITE; PDOC00585; PROSITE; PDOC00685;
PDB	2VYC; 3NZP; 3ZNQ;
Organisms	-Eubacteria -Archea -Plants -Metazoa -Human
Family	4.1.1.19_1 (29) 4.1.1.19_2 (10)

Links	Enzyme (activities) 4.1.1.19 BRENDA (activities) 4.1.1.19 KEGG (pathways) 4.1.1.19 PLPMDB (PLP mutants) 4.1.1.19

References	Alam M, Srivastava A, Dutta A, Sau AK (2018) Biochemical and biophysical studies of Helicobacter pylori arginine decarboxylase, an enzyme important for acid adaptation in host IUBMB Life 70 658-669. Docimo T, Reichelt M, Schneider B, Kai M, Kunert G, Gershenzon J, D'Auria JC. (2012) The first step in the biosynthesis of cocaine in Erythroxylum coca: the characterization of arginine and ornithine decarboxylases. Plant Mol Biol. 78 599-615. Forouhar F1, Lew S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Tong L. (2010) Structures of bacterial biosynthetic arginine decarboxylases. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66 1562-6. Giles TN, Graham DE. (2008) Crenarchaeal arginine decarboxylase evolved from an S-adenosylmethionine decarboxylase enzyme J Biol Chem 283 25829-38. Counts KG, Wong I, Oliveira MA (2007) Investigating the geminal diamine intermediate of Yersinia pestis arginine decarboxylase with substrate, product, and inhibitors using single wavelength stopped-flow spectroscopy Biochemistry 46 379-86. Lu CD, Yang Z, Li W. (2004) Transcriptome analysis of the ArgR regulon in Pseudomonas aeruginosa J Bacteriol 186 3855-61. Hanfrey, C.; Sommer, S.; Mayer, M.J., Burtin, D., Michael, A.J. (2001) Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity Plant J 27 551-60. Sekowska, A.; Bertin, P.; Danchin, A. (1998) Characterization of polyamine synthesis pathway in Bacillus subtilis 168 Mol Microbiol 29 851-8. Stim, K.P.; Bennett, G.N. (1993) Nucleotide sequence of the adi gene, which encodes the biodegradative acid-induced arginine decarboxylase of Escherichia coli J Bacteriol 175 1221-34. Bell, E.; Malmberg, R.L. (1990) Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence of protein processing Mol Gen Genet 224 431-6. Moore, R. C.; Boyle, S. M. (1990) Nucleotide sequence and analysis of the speA gene encoding biosynthetic arginine decarboxylase in Escherichia coli J Bacteriol 172 4631-40. Articles on 4.1.1.19

last changed	2019/06/20 13:40

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