EC 4.1.1.12 - Aspartate 4-decarboxylase

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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
Systematic name:
L-aspartate 4-carboxy-lyase (L-alanine-forming)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0047688
CAS Registry Number: 9024-57-1
UniProtKB/Swiss-Prot:

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: 353-358 (1969). [PMID: 5773301]
  2. Novogrodsky, A. and Meister, A.
    Control of aspartate β-decarboxylase activity by transamination.
    J. Biol. Chem. 239: 879-888 (1964).
  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: 2310-2315 (1970). [PMID: 5424207]
  4. Wilson, E.M. and Kornberg, H.L.
    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)]