EC 4.1.1.12 - Aspartate 4-decarboxylase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 4.1.1.12
Names
Accepted name:
aspartate 4-decarboxylase
Other
names:
L-aspartate β-decarboxylase
L-cysteine sulfinate acid desulfinase
aminomalonic decarboxylase
aspartate β-decarboxylase
aspartate ω-decarboxylase
aspartic β-decarboxylase
aspartic ω-decarboxylase
cysteine sulfinic desulfinase
desulfinase
L-aspartate 4-carboxy-lyase
L-cysteine sulfinate acid desulfinase
aminomalonic decarboxylase
aspartate β-decarboxylase
aspartate ω-decarboxylase
aspartic β-decarboxylase
aspartic ω-decarboxylase
cysteine sulfinic desulfinase
desulfinase
L-aspartate 4-carboxy-lyase
Systematic name:
L-aspartate 4-carboxy-lyase (L-alanine-forming)
Reaction
- L-aspartate = L-alanine + CO2
Cofactor
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
Gene Ontology:
GO:0047688
CAS Registry Number:
9024-57-1
UniProtKB/Swiss-Prot:
References
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Crystalline L-aspartate β-decarboxylase of Pseudomonas dacunhae. I. Crystallization and some physiocochemical properties.J. Biol. Chem. 244 : 353-358 (1969). [PMID: 5773301]
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Control of aspartate β-decarboxylase activity by transamination.J. Biol. Chem. 239 : 879-888 (1964).
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Inhibition of aspartate β-decarboxylase by aminomalonate. Stereospecific decarboxylation of aminomalonate to glycine.Biochemistry 9 : 2310-2315 (1970). [PMID: 5424207]
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Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp.Biochem. J. 88 : 578-587 (1963).
[EC 4.1.1.12 created 1961, modified 1976 (EC 4.1.1.10 created 1961, incorporated 1972)]