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Isobutyryl-CoA mutase

From Wikipedia, the free encyclopedia
isobutyryl-CoA mutase
Identifiers
EC no.5.4.99.13
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

In enzymology, an isobutyryl-CoA mutase (EC 5.4.99.13) is an enzyme that catalyzes the chemical reaction

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

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  • 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.