EC |
7.2.4.2 |
Accepted name: |
oxaloacetate decarboxylase (Na+ extruding) |
Reaction: |
oxaloacetate + 2 Na+[side 1] = pyruvate + CO2 + 2 Na+[side 2] |
Other name(s): |
oxaloacetate β-decarboxylase (ambiguous); oxalacetic acid decarboxylase (ambiguous); oxalate β-decarboxylase (ambiguous); oxaloacetate carboxy-lyase (ambiguous) |
Systematic name: |
oxaloacetate carboxy-lyase (pyruvate-forming; Na+-extruding) |
Comments: |
The enzyme from the bacterium Klebsiella aerogenes is a biotinyl protein and also decarboxylates glutaconyl-CoA and methylmalonyl-CoA. The process is accompanied by the extrusion of two sodium ions from cells. Some animal enzymes require Mn2+. Differs from EC 4.1.1.112 (oxaloacetate decarboxylase) for which there is no evidence for involvement in Na+ transport. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9024-98-0 |
References: |
1. |
Dimroth, P. Characterization of a membrane-bound biotin-containing enzyme: oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 115 (1981) 353–358. [DOI] [PMID: 7016536] |
2. |
Dimroth, P. The role of biotin and sodium in the decarboxylation of oxaloacetate by the membrane-bound oxaloacetate decarboxylase from Klebsiella aerogenes. Eur. J. Biochem. 121 (1982) 435–441. [DOI] [PMID: 7037395] |
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[EC 7.2.4.2 created 1961 as EC 4.1.1.3, modified 1986, modified 2000, transferred 2018 to EC 7.2.4.2] |
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