Aspartate 4-decarboxylase
In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction
| aspartate 4-decarboxylase | |
|---|---|
Aspartate beta-decarboxylase dodekamer, Comamonas testosteroni | |
| Identifiers | |
| EC no. | 4.1.1.12 |
| CAS no. | 9024-57-1 |
| Databases | |
| IntEnz | IntEnz view |
| BRENDA | BRENDA entry |
| ExPASy | NiceZyme view |
| KEGG | KEGG entry |
| MetaCyc | metabolic pathway |
| PRIAM | profile |
| PDB structures | RCSB PDB PDBe PDBsum |
| Gene Ontology | AmiGO / QuickGO |
- L-aspartate L-alanine + CO2
Hence, this enzyme has one substrate, L-aspartate, and two products, L-alanine and CO2. This reaction is the basis of the industrial synthesis of L-alanine.[1]
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is L-aspartate 4-carboxy-lyase (L-alanine-forming). Other names in common use include desulfinase, aminomalonic decarboxylase, aspartate beta-decarboxylase, aspartate omega-decarboxylase, aspartic omega-decarboxylase, aspartic beta-decarboxylase, L-aspartate beta-decarboxylase, cysteine sulfinic desulfinase, L-cysteine sulfinate acid desulfinase, and L-aspartate 4-carboxy-lyase. This enzyme participates in alanine and aspartate metabolism and cysteine metabolism. It employs one cofactor, pyridoxal phosphate.
References edit
- ^ Karlheinz Drauz, Ian Grayson, Axel Kleemann, Hans-Peter Krimmer, Wolfgang Leuchtenberger, Christoph Weckbecker (2006). Ullmann's Encyclopedia of Industrial Chemistry. Weinheim: Wiley-VCH. doi:10.1002/14356007.a02_057.pub2. ISBN 978-3527306732.
{{cite encyclopedia}}: CS1 maint: multiple names: authors list (link)
- Kakimoto T, Kato J, Shibatani T, Nishimura N, Chibata I (1969). "Crystalline L-aspartate beta-decarboxylase of Pseudomonas dacunhae I. Crystallization and some physiocochemical properties". J. Biol. Chem. 244 (2): 353–8. doi:10.1016/S0021-9258(18)94438-8. PMID 5773301.
- Novogrodsky A; Meister A (1964). "Control of aspartate beta-decarboxylase activity by transamination". J. Biol. Chem. 239 (3): 879–888. doi:10.1016/S0021-9258(18)51672-0. PMID 14154469.
- Palekar AG, Tate SS, Meister A (1970). "Inhibition of aspartate beta-decarboxylase by aminomalonate Stereospecific decarboxylation of aminomalonate to glycine". Biochemistry. 9 (11): 2310–5. doi:10.1021/bi00813a014. PMID 5424207.
- Wilson EM; Kornberg HL (1963). "Properties of crystalline l-aspartate 4-carboxy-lyase from Achromobacter sp". Biochem. J. 88 (3): 578–587. doi:10.1042/bj0880578. PMC 1202217. PMID 14071532.