2-methylacyl-CoA dehydrogenase
2-methylacyl-CoA dehydrogenase | |||||||||
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Identifiers | |||||||||
EC number | 1.3.99.12 | ||||||||
CAS number | 85130-32-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / EGO | ||||||||
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In enzymology, a 2-methylacyl-CoA dehydrogenase (EC 1.3.99.12) is an enzyme that catalyzes the chemical reaction
- 2-methylbutanoyl-CoA + acceptor 2-methylbut-2-enoyl-CoA + reduced acceptor
Thus, the two substrates of this enzyme are 2-methylbutanoyl-CoA and acceptor, whereas its two products are 2-methylbut-2-enoyl-CoA and reduced acceptor.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with other acceptors. The systematic name of this enzyme class is 2-methylbutanoyl-CoA:acceptor oxidoreductase. Other names in common use include branched-chain acyl-CoA dehydrogenase, 2-methyl branched chain acyl-CoA dehydrogenase, and 2-methylbutanoyl-CoA:(acceptor) oxidoreductase. This enzyme participates in valine, leucine and isoleucine degradation.
References
- Ikeda Y, Dabrowski C, Tanaka K (1983). "Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066–76. PMID 6401712.
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