Aspartate 4-decarboxylase

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In enzymology, an aspartate 4-decarboxylase (EC 4.1.1.12) is an enzyme that catalyzes the chemical reaction

L-aspartate $\rightleftharpoons$ L-alanine + CO₂

Hence, this enzyme has one substrate, L-aspartate, and two products, L-alanine and CO₂.

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.

[edit] References

IUBMB entry for 4.1.1.12
BRENDA references for 4.1.1.12 (Recommended.)
PubMed references for 4.1.1.12
PubMed Central references for 4.1.1.12
Google Scholar references for 4.1.1.12
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: 353–8. PMID 5773301.
Novogrodsky A and Meister A (1964). "Control of aspartate beta-decarboxylase activity by transamination". J. Biol. Chem. 239: 879–888.
Palekar AG, Tate SS, Meister A (1970). "Inhibition of aspartate beta-decarboxylase by aminomalonate Stereospecific decarboxylation of aminomalonate to glycine". Biochemistry. 9: 2310–5. doi:10.1021/bi00813a014. PMID 5424207.
Wilson EM and Kornberg HL (1963). "Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp". Biochem. J. 88: 578–587.