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
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b12-dependent
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mutases
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acyl-coas
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n-butyryl-coa
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cinnamonensis
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icmfs
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polyketide
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succinyl-coa
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monensin
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isomerases
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meaa
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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
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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
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5\'-deoxyadenosyl
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coa-dependent
- isobutanol
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methylmalonyl
- methylobacterium
- crotonyl-coa
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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
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General Information
General Information on EC 5.4.99.13 - isobutyryl-CoA mutase
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evolution
physiological function
additional information
enzyme IcmF belongs to the family of adenosylcobalamin-dependent isomerases, whose members catalyze carbon skeleton rearrangements using radical chemistry
evolution
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enzyme IcmF belongs to the family of adenosylcobalamin-dependent isomerases, whose members catalyze carbon skeleton rearrangements using radical chemistry
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IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with isomerase activity. IcmF is prone to inactivation during catalytic turnover, thus setting up its dependence on a cofactor repair system. The GTPase activity of IcmF powers the ejection of the inactive cob(II)alamin cofactor and requires the presence of an acceptor protein, adenosyltransferase, for receiving it. Adenosyltransferase in turn converts cob(II)alamin to AdoCbl in the presence of ATP and a reductant. The repaired cofactor is then reloaded onto IcmF in a GTPase-gated step. The mechanistic details of cofactor loading and offloading from the AdoCbl-dependent IcmF are distinct from those of the homologous methylmalonyl-CoA mutase/G-protein chaperone system, overview
physiological function
the isobutyryl-CoA mutase variant, IcmF, catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA and it also catalyzes the interconversion between isovaleryl-CoA and pivalyl-CoA, albeit with low efficiency and high susceptibility to inactivation
physiological function
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the isobutyryl-CoA mutase variant, IcmF, catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA and it also catalyzes the interconversion between isovaleryl-CoA and pivalyl-CoA, albeit with low efficiency and high susceptibility to inactivation
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physiological function
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IcmF is a 5'-deoxyadenosylcobalamin (AdoCbl)-dependent enzyme that catalyzes the carbon skeleton rearrangement of isobutyryl-CoA to butyryl-CoA. It is a bifunctional protein resulting from the fusion of a G-protein chaperone with GTPase activity and the cofactor- and substrate-binding mutase domains with isomerase activity. IcmF is prone to inactivation during catalytic turnover, thus setting up its dependence on a cofactor repair system. The GTPase activity of IcmF powers the ejection of the inactive cob(II)alamin cofactor and requires the presence of an acceptor protein, adenosyltransferase, for receiving it. Adenosyltransferase in turn converts cob(II)alamin to AdoCbl in the presence of ATP and a reductant. The repaired cofactor is then reloaded onto IcmF in a GTPase-gated step. The mechanistic details of cofactor loading and offloading from the AdoCbl-dependent IcmF are distinct from those of the homologous methylmalonyl-CoA mutase/G-protein chaperone system, overview
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enzyme IcmF in general is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone. IcmF from Cupriavidus metallidurans, which also contains a G-protein domain in addition to the mutase domains, with AdoCbl in the ICM active site and GDP-Mg2+ in the G-protein active site (holo-IcmF-GDP)
additional information
GDP binding by the enzyme is accompanied by favorable enthalpic and entropic changes and is unaffected by 5'-deoxyadenosylcobalamin
additional information
IcmF is a natural variant in which the small and large subunits found in ICM are fused via a middle G-protein chaperone domain, active site sequence comparisons, overview
additional information
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IcmF is a natural variant in which the small and large subunits found in ICM are fused via a middle G-protein chaperone domain, active site sequence comparisons, overview
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additional information
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enzyme IcmF in general is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone. IcmF from Cupriavidus metallidurans, which also contains a G-protein domain in addition to the mutase domains, with AdoCbl in the ICM active site and GDP-Mg2+ in the G-protein active site (holo-IcmF-GDP)
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additional information
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GDP binding by the enzyme is accompanied by favorable enthalpic and entropic changes and is unaffected by 5'-deoxyadenosylcobalamin
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