In enzymology, an isobutyryl-CoA mutase (EC 5.4.99.13) is an enzyme that catalyzes the chemical reaction
| isobutyryl-CoA mutase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.4.99.13 | ||||||||
| 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 / QuickGO | ||||||||
| |||||||||
- 2-methylpropanoyl-CoA butanoyl-CoA
Hence, this enzyme has one substrate, 2-methylpropanoyl-CoA, and one product, butanoyl-CoA.
This enzyme belongs to the family of isomerases, specifically those intramolecular transferases transferring other groups. The systematic name of this enzyme class is 2-methylpropanoyl-CoA CoA-carbonylmutase. Other names in common use include isobutyryl coenzyme A mutase, and butyryl-CoA:isobutyryl-CoA mutase. It uses adenosylcobalamin as a cofactor, which is bound at the enzyme's vitamin B12-binding domain. The mechanism of action of the enzyme is to generate a 5′-deoxyadenosyl radical by homolytic cleavage of the cobalt-carbon bond of the cofactor. This radical abstracts a hydrogen atom from the substrate to initiate the rearrangement reaction.
References
edit- Brendelberger G, Rétey J, Ashworth DM, Reynolds K, Willenbrock F, Robinson JA (1988). "The Enzymic Interconversion of Isobutyryl and n-Butyrylcarba(dethia)-Coenzyme A: A Coenzyme-B12-dependent Carbon Skeleton Rearrangement". Angewandte Chemie International Edition in English. 27 (8): 1089–1090. doi:10.1002/anie.198810891.
- Jost M, Born DA, Cracan V, Banerjee R, Drennan CL (November 2015). "Structural Basis for Substrate Specificity in Adenosylcobalamin-dependent Isobutyryl-CoA Mutase and Related Acyl-CoA Mutases". The Journal of Biological Chemistry. 290 (45): 26882–26898. doi:10.1074/jbc.M115.676890. PMC 4646380. PMID 26318610.
