| EC |
4.1.1.12 |
| Accepted name: |
aspartate 4-decarboxylase |
| Reaction: |
L-aspartate = L-alanine + CO2 |
| Other name(s): |
desulfinase; aminomalonic decarboxylase; aspartate β-decarboxylase; aspartate ω-decarboxylase; aspartic ω-decarboxylase; aspartic β-decarboxylase; L-aspartate β-decarboxylase; cysteine sulfinic desulfinase; L-cysteine sulfinate acid desulfinase; L-aspartate 4-carboxy-lyase |
| Systematic name: |
L-aspartate 4-carboxy-lyase (L-alanine-forming) |
| Comments: |
A pyridoxal-phosphate protein. Also catalyses the decarboxylation of aminomalonate (formerly listed as EC 4.1.1.10), and the desulfination of 3-sulfino-L-alanine to sulfite and alanine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-57-1 |
| References: |
| 1. |
Kakimoto, T., Kato, J., Shibitani, T., Nishimura, N. and Chibata, I. Crystalline L-aspartate β-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties. J. Biol. Chem. 244 (1969) 353–358. [PMID: 5773301] |
| 2. |
Novogrodsky, A. and Meister, A. Control of aspartate β-decarboxylase activity by transamination. J. Biol. Chem. 239 (1964) 879–888. [PMID: 14154469] |
| 3. |
Palekar, A.G., Tate, S.S. and Meister, A. Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine. Biochemistry 9 (1970) 2310–2315. [PMID: 5424207] |
| 4. |
Wilson, E.M. and Kornberg, H.L. Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp. Biochem. J. 88 (1963) 578–587. [PMID: 14071532] |
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| [EC 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)] |
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