5.4.99.13: isobutyryl-CoA mutase
This is an abbreviated version!
For detailed information about isobutyryl-CoA mutase, go to the full flat file.
Word Map on EC 5.4.99.13
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5.4.99.13
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methylmalonyl-coa
-
b12-dependent
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mutases
-
acyl-coas
-
n-butyryl-coa
-
cinnamonensis
-
icmfs
-
polyketide
-
succinyl-coa
-
monensin
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isomerases
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meaa
-
5'-deoxyadenosylcobalamin-dependent
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2-hydroxyisobutyrate
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extorquens
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isobutyrate
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cobiialamin
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2r-methylmalonyl-coa
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synthesis
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b12-binding
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mutase-catalyzed
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5'-deoxyadenosine
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5\'-deoxyadenosyl
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coa-dependent
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isobutanol
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methylmalonyl
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methylobacterium
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crotonyl-coa
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pivalic
-
biofuel production
- 5.4.99.13
- methylmalonyl-coa
-
b12-dependent
- mutases
- acyl-coas
- n-butyryl-coa
- cinnamonensis
-
icmfs
- polyketide
- succinyl-coa
- monensin
- isomerases
- meaa
-
5'-deoxyadenosylcobalamin-dependent
- 2-hydroxyisobutyrate
- extorquens
- isobutyrate
-
cobiialamin
-
2r-methylmalonyl-coa
- synthesis
-
b12-binding
-
mutase-catalyzed
- 5'-deoxyadenosine
-
5\'-deoxyadenosyl
-
coa-dependent
- isobutanol
-
methylmalonyl
- methylobacterium
- crotonyl-coa
-
pivalic
- biofuel production
Reaction
Synonyms
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, pivalyl-CoA mutase
ECTree
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Systematic Name
Systematic Name on EC 5.4.99.13 - isobutyryl-CoA mutase
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2-methylpropanoyl-CoA CoA-carbonylmutase
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 2.5.1.17, 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.