5.4.99.64: 2-hydroxyisobutanoyl-CoA mutase
This is an abbreviated version!
For detailed information about 2-hydroxyisobutanoyl-CoA mutase, go to the full flat file.
Word Map on EC 5.4.99.64
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5.4.99.64
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b12-dependent
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aquincola
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tertiaricarbonis
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acyl-coa
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s-3-hydroxybutyryl-coa
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2-hydroxyisobutyric
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chaperone
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mutases
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2-hydroxyisobutyrylation
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isomerization
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isovaleryl-coa
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tert-butyl
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thioester
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synthesis
- 5.4.99.64
-
b12-dependent
-
aquincola
- tertiaricarbonis
- acyl-coa
-
s-3-hydroxybutyryl-coa
-
2-hydroxyisobutyric
- chaperone
- mutases
-
2-hydroxyisobutyrylation
-
isomerization
- isovaleryl-coa
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tert-butyl
- thioester
- synthesis
Reaction
Synonyms
2-hydroxyisobutyryl-CoA mutase, Btus_0469, Btus_0470, EC 5.3.3.20, HCM, HcmA, hcmAB, HcmB, RcmA, RcmB
ECTree
5.4.99.64 2-hydroxyisobutanoyl-CoA mutaseAdvanced search results
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results (Engineering
Engineering on EC 5.4.99.64 - 2-hydroxyisobutanoyl-CoA mutase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D117A
D117V
I90A
I90L
I90V
I90V
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significant activities are only obtained with (S)-3-hydroxybutanoyl- and 2-hydroxyisobutanoyl-CoA, showing less than 20% of the wild-type rates. The substitution I90V results in Km values close to 2 mM and a nearly 100fold diminution of the catalytic efficiency with (S)-3-hydroxybuytryl-CoA
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D117A
mutation in the large subunit HcmA results in significantly increased activity toward (R)-3-hydroxybutyryl-CoA
D117A
mutation in subunit HcmA, results in significantly increased activity toward (R)-3-hydroxybutyryl-CoA
D117V
mutation in the large subunit HcmA results in significantly increased activity toward (R)-3-hydroxybutyryl-CoA. The mutant enzyme shows high activity toward pivalyl-CoA
D117V
mutation in subunit HcmA, results in significantly increased activity toward (R)-3-hydroxybutyryl-CoA and high activity toward pivalyl-CoA
I90A
mutation in the large subunit HcmA results in a significant reduction in conversion rates and diminution of the catalytic efficiencies for the main substrates of the wild-type enzyme, (S)-3-hydroxybutyryl-coA and 2-hydroxyisobutyryl-CoA. Wild-type enzyme as well as mutant enzyme can also isomerize pivalyl- and isovaleryl-CoA, albeit at more than 10times lower rates than the favorite substrate (S)-3-hydroxybutyryl-CoA
I90L
mutation in the large subunit HcmA results in a significant reduction in conversion rates and diminution of the catalytic efficiencies for the main substrates of the wild-type enzyme, (S)-3-hydroxybutyryl-coA and 2-hydroxyisobutyryl-CoA. Mutant enzyme does not show any significant activities with pivalyl-CoA and isovaleryl-CoA
I90V
significant activities are only obtained with (S)-3-hydroxybutanoyl- and 2-hydroxyisobutanoyl-CoA, showing less than 20% of the wild-type rates. The substitution I90V results in Km values close to 2 mM and a nearly 100fold diminution of the catalytic efficiency with (S)-3-hydroxybuytryl-CoA
I90V
mutation in the large subunit HcmA, wild-type enzyme as well as mutant enzyme can also isomerize pivalyl- and isovaleryl-CoA, albeit at more than 10times lower rates than the favorite substrate (S)-3-hydroxybutyryl-CoA
