Information on EC - isobutyryl-CoA mutase

for references in articles please use BRENDA:EC5.4.99.13
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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
       isobutyryl-CoA mutase
IUBMB Comments
This bacterial enzyme utilizes 5'-deoxyadenosylcobalamin as a cofactor. Following substrate binding, the enzyme catalyses the homolytic cleavage of the cobalt-carbon bond of AdoCbl, yielding cob(II)alamin and a 5'-deoxyadenosyl radical, which initiates the the carbon skeleton rearrangement reaction by hydrogen atom abstraction from the substrate. At the end of each catalytic cycle the 5'-deoxyadenosyl radical and cob(II)alamin recombine, regenerating the resting form of the cofactor. The enzyme is prone to inactivation resulting from occassional loss of the 5'-deoxyadenosyl molecule. Inactivated enzymes are repaired by the action of EC, cob(I)yrinic acid a,c-diamide adenosyltransferase, and a G-protein chaperone, which restore cob(II)alamin (which is first reduced to cob(I)alamin by an unidentified reductase) to 5'-deoxyadenosylcobalamin and load it back on the mutase. Some mutases are fused with their G-protein chaperone. These enzyme can also catalyse the interconversion of isovaleryl-CoA with pivalyl-CoA.
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The enzyme appears in viruses and cellular organisms
adenosylcobalamin-dependent isobutyryl-CoA mutase, AdoCbl-dependent PCM, butyryl-CoA:isobutyryl-CoA mutase, CmIcmF, ICM, IcmF, isobutyryl coenzyme A mutase, isobutyryl-CoA mutase fused, isovaleryl-CoA/pivalyl-CoA mutase, PCM, more
2-methylpropanoyl-CoA = butanoyl-CoA
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