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
-
mutases
-
acyl-coas
-
n-butyryl-coa
-
cinnamonensis
-
icmfs
-
polyketide
-
succinyl-coa
-
monensin
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isomerases
-
meaa
-
5'-deoxyadenosylcobalamin-dependent
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2-hydroxyisobutyrate
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extorquens
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isobutyrate
-
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
-
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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Molecular Weight
Molecular Weight on EC 5.4.99.13 - isobutyryl-CoA mutase
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135000
recombinant detagged enzyme, large subunit dimer, gel filtration
14300
alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain
20000
recombinant detagged enzyme, small subunit monomer, gel filtration
62500
alpha2beta2, IcmA2IcmB2, 2 * 62500 + 2 * 14300, gel filtration, IcmB provides the cobalamin-binding domain
additional information
size exclusion chromatography yields an estimated molecular mass of 135 kDa, consistent with the large subunit being a homodimer. The recombinant small subunit of PCM is purified as N-terminally His6-tagged protein and elutes with an apparent mass of 20 kDa in gel filtration, suggesting that it exists as a monomer based on the predicted mass of the polypeptide of 17.7 kDa. Gel filtration of a 1:1 mixture of the large and small subunits ofthe enzyme in presence of 5'-deoxyadenosylcobalamin, shows no evidence of complex formation, indicating weak interaction between the subunits under these conditions