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4.1.1.19 |
Description |
Arginine decarboxylase |
Catalyzed reaction |
L-arginine = agmatine + CO(2). |
Cofactor |
Pyridoxal-phosphate or pyruvate. |
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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 |
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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
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References |
Articles on 4.1.1.19 |
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last changed |
2019/06/20 13:40 |
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