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4.1.1.12 |
| Description |
Aspartate 4-decarboxylase. |
| Alternative names |
Cysteine sulfinate desulfinase. |
| Catalyzed reaction |
L-aspartate = L-alanine + CO(2). |
| Cofactor |
Pyridoxal-phosphate. |
| Comments |
-!- Also catalyzes the decarboxylation of aminomalonate and the desulfination of 3-sulfino-L-alanine to sulfite and alanine. -!- Formerly EC 4.1.1.10. |
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The only validated sequences are from bacteria. The activity occurs also in fungi and metazoa (the rat enzyme appears to be membrane-bound) but no sequences similar to the bacterial ones are found in the genomes of these organisms. |
| Organisms |
-Bacteria -Fungi -Metazoa |
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Family |
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| Links |
Enzyme (activities) 4.1.1.12
BRENDA (activities) 4.1.1.12
KEGG (pathways) 4.1.1.12
PLPMDB (PLP mutants) 4.1.1.12
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| References |
Wang NC, Lee CY. (2006) Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas sp. ATCC 19121 and characterization of the bifunctional recombinant enzyme Appl Microbiol Biotechnol 73 339-48. Abe, K.; Ohnishi, F.; Yagi, K.; Nakajima, T.; Higuchi, T.; Sano, M.; Machida, M.; Sarker, R.I.; Maloney, P.C. (2002) Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction J Bacteriol 184 2906-13. Chen, C-C.
Chou, T-L.
Lee, C-Y. (2000) Cloning, expression and characterization of L-aspartate beta-decarboxylase gene from Alcaligenes faecalis CCRC 11585 J Industrial Microbiol Biotechnol 25 132-140. Articles on 4.1.1.12 |
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| last changed |
2007/12/21 19:05 |
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