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Information on EC 5.4.99.64 - 2-hydroxyisobutanoyl-CoA mutase
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EC Tree
5.4.99.64 2-hydroxyisobutanoyl-CoA mutaseIUBMB Comments
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety.
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Word Map
- 5.4.99.64
-
b12-dependent
-
aquincola
- tertiaricarbonis
- acyl-coa
-
s-3-hydroxybutyryl-coa
-
2-hydroxyisobutyric
- chaperone
- mutases
-
2-hydroxyisobutyrylation
-
isomerization
- isovaleryl-coa
-
tert-butyl
- thioester
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
2-hydroxyisobutyryl-coa mutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxyisobutyryl-CoA mutase
EC 5.3.3.20
-
-
formerly
-
HcmA
hcmAB
HcmB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxy-2-methylpropanoyl-CoA = (S)-3-hydroxybutanoyl-CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxy-2-methylpropanoyl-CoA mutase
The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-3-hydroxybutanoyl-CoA
2-hydroxybutanoyl-CoA
D5WTR7; D5WTR8
catalytic efficiency for the (R)-enantiomer is about 11 times higher than for the (S)-enantiomer
-
-
r
(S)-3-hydroxybutanoyl-CoA
2-hydroxybutanoyl-CoA
D5WTR7; D5WTR8
catalytic efficiency for the (R)-enantiomer is about 11 times higher than for the (S)-enantiomer
-
-
r
2,2-dimethylpropanoyl-CoA
?
wild-type enzyme as well as I90V (HcmA) and I90A (HcmA) mutant enzymes can also isomerize pivaloyl-CoA and isovaleryl-CoA, albeit at more than 10times lower rates than the favorite substrate (S)-3-hydroxybutyryl-CoA
-
-
r
2-hydroxyisobutanoyl-CoA
(S)-3-hydroxyisobutanoyl-CoA + (R)-3-hydroxyisobutanoyl-CoA
D5WTR7; D5WTR8
-
-
-
r
butanoyl-CoA
isobutanoyl-CoA
low rearrangement activity, corresponding to approximately 2% of the (S)-3-hydroxybutanoyl-CoA conversion rate
-
-
r
isovaleryl-CoA
?
wild-type enzyme as well as I90V (HcmA) and I90A (HcmA) mutant enzymes can also isomerize pivalyl- and isovaleryl-CoA, albeit at more than 10times lower rates than the favorite substrate (S)-3-hydroxybutyryl-CoA
-
-
?
isovaleryl-CoA
pentanoyl-CoA
at 10 times lower rate than substrate (S)-3-hydroxybutanoyl-CoA
-
-
r
pivaloyl-CoA
?
at 10 times lower rate than substrate (S)-3-hydroxybutanoyl-CoA
-
-
r
(R)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
poor substrate
-
-
r
(R)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
2-hydroxy-2-methylpropanoyl i.e. 2-hydroxyisobutanoyl-CoA. 2-Hydroxyisobutanoyl-CoA is predominantly converted to (S)-3-hydroxybutanoyl-CoA, and only minor amounts of about 20% of the (R)-enantiomer are obtained
-
-
r
(R)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
very low activity with wild-type enzyme. Mutations D117V or D117A in the large subunit HcmA result in significantly increased activity toward (R)-3-hydroxybutyryl-CoA
-
-
r
(R)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
2-hydroxy-2-methylpropanoyl i.e. 2-hydroxyisobutanoyl-CoA. 2-Hydroxyisobutanoyl-CoA is predominantly converted to (S)-3-hydroxybutanoyl-CoA, and only minor amounts of about 20% of the (R)-enantiomer are obtained
-
-
r
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
-
-
-
r
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
favorite substrate
-
-
r
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl-CoA
-
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
-
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
the enzym plays a central role in the degradation of assorted substrates containing a tert-butyl moiety
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl i.e. 2-hydroxyisobutanoyl-CoA. 2-Hydroxyisobutanoyl-CoA is predominantly converted to (S)-3-hydroxybutanoyl-CoA, and only minor amounts of about 20% of the (R)-enantiomer are obtained, indicating stereospecific catalysis. The enzyme uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. Compared with Vmax obtained with 2-hydroxyisobutanoyl-CoA, rates with (S)-3-hydroxybutanoyl-CoA are nearly four times higher
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
the enzym plays a central role in the degradation of assorted substrates containing a tert-butyl moiety
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
2-hydroxy-2-methylpropanoyl i.e. 2-hydroxyisobutanoyl-CoA. 2-Hydroxyisobutanoyl-CoA is predominantly converted to (S)-3-hydroxybutanoyl-CoA, and only minor amounts of about 20% of the (R)-enantiomer are obtained, indicating stereospecific catalysis. The enzyme uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. Compared with Vmax obtained with 2-hydroxyisobutanoyl-CoA, rates with (S)-3-hydroxybutanoyl-CoA are nearly four times higher
-
-
r
isobutanoyl-CoA
butanoyl-CoA
low rearrangement activity, corresponding to approximately 0.5% of the (S)-3-hydroxybutanoyl-CoA conversion rate
-
-
r
additional information
?
-
the enzyme does not show detectable conversion of methylmalonyl-CoA and succinyl-CoA
-
-
?
additional information
?
-
-
the enzyme does not show detectable conversion of methylmalonyl-CoA and succinyl-CoA
-
-
?
additional information
?
-
the enzyme does not show detectable conversion of methylmalonyl-CoA and succinyl-CoA
-
-
?
additional information
?
-
D5WTR7; D5WTR8
(R)-3-hydroxybuytryl-CoA is converted 3.1 times faster than the (S)-enantiomer
-
-
?
additional information
?
-
-
(R)-3-hydroxybuytryl-CoA is converted 3.1 times faster than the (S)-enantiomer
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
the enzym plays a central role in the degradation of assorted substrates containing a tert-butyl moiety
-
-
r
2-hydroxy-2-methylpropanoyl-CoA
(S)-3-hydroxybutanoyl-CoA
the enzym plays a central role in the degradation of assorted substrates containing a tert-butyl moiety
-
-
r
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cobalamin
the smaller one of the two subunits (hcmB) contains a cobalamin cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
isobutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.0075
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.008
(R)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.067
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.067
(R)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.298
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.298
(R)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
1.66
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
1.66
(R)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
0.0146
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.015
(S)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.117
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.117
(S)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.128
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.128
(S)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
0.433
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme, I90A (mutation in subunit HcmA)
0.433
(S)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.663
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.663
(S)-3-hydroxybutanoyl-CoA
mutant I90L, pH 6.6, 30°C
1.76
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
1.76
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
1.76
(S)-3-hydroxybutanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.0435
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.235
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.374
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.977
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.042
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.042
2-hydroxy-2-methylpropanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.061
2-hydroxy-2-methylpropanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.0614
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.104
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.104
2-hydroxy-2-methylpropanoyl-CoA
-
pH 6.6, 30°C, wild-type enzyme
0.104
2-hydroxy-2-methylpropanoyl-CoA
wild-type, pH 6.6, 30°C
0.304
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.304
2-hydroxy-2-methylpropanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.517
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.517
2-hydroxy-2-methylpropanoyl-CoA
mutant I90L, pH 6.6, 30°C
1.84
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
1.84
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
1.84
2-hydroxy-2-methylpropanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.147
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.288
isovaleryl-CoA
pH 6.6, 30°C, wild-type enzyme
0.329
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
isobutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.003
(R)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
0.0033
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.0035
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.004
(R)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.027
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.027
(R)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.17
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.173
(R)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.002
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.002
(S)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.003
(S)-3-hydroxybutanoyl-CoA
mutant I90L, pH 6.6, 30°C
0.0035
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.0255
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.026
(S)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.033
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
0.033
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.033
(S)-3-hydroxybutanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.062
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.062
(S)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.2
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.2
(S)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
0.013
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.016
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.017
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.14
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.0067
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.007
2-hydroxy-2-methylpropanoyl-CoA
mutant I90L, pH 6.6, 30°C
0.02
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
0.02
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.02
2-hydroxy-2-methylpropanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.0245
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.025
2-hydroxy-2-methylpropanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.044
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.044
2-hydroxy-2-methylpropanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.045
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.045
2-hydroxy-2-methylpropanoyl-CoA
mutant D117V, pH 6.6, 30°C
0.05
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.05
2-hydroxy-2-methylpropanoyl-CoA
-
pH 6.6, 30°C, wild-type enzyme
0.05
2-hydroxy-2-methylpropanoyl-CoA
wild-type, pH 6.6, 30°C
0.009
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.0093
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.011
isovaleryl-CoA
pH 6.6, 30°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
isobutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.00199
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.002
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.002
(R)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
0.012
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.012
(R)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
2.583
(R)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
2.6
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
3.667
(R)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
3.7
(R)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
0.0047
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme, I90A (mutation in subunit HcmA)
0.005
(S)-3-hydroxybutanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.005
(S)-3-hydroxybutanoyl-CoA
mutant I90L, pH 6.6, 30°C
0.0052
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.018
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.018
(S)-3-hydroxybutanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.019
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
0.525
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.525
(S)-3-hydroxybutanoyl-CoA
mutant D117V, pH 6.6, 30°C
1.5
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
1.5
(S)-3-hydroxybutanoyl-CoA
wild-type, pH 6.6, 30°C
1.56
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
1.75
(S)-3-hydroxybutanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
1.75
(S)-3-hydroxybutanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.017
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.043
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.057
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
3.2
2,2-dimethylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.011
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V
0.012
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.012
2-hydroxy-2-methylpropanoyl-CoA
mutant I90V, pH 6.6, 30°C
0.013
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90L (mutation in subunit HcmA)
0.013
2-hydroxy-2-methylpropanoyl-CoA
mutant I90L, pH 6.6, 30°C
0.082
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme I90A (mutation in subunit HcmA)
0.082
2-hydroxy-2-methylpropanoyl-CoA
mutant I90A, pH 6.6, 30°C
0.48
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, wild-type enzyme
0.48
2-hydroxy-2-methylpropanoyl-CoA
-
pH 6.6, 30°C, wild-type enzyme
0.48
2-hydroxy-2-methylpropanoyl-CoA
wild-type, pH 6.6, 30°C
0.727
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
0.727
2-hydroxy-2-methylpropanoyl-CoA
mutant D117V, pH 6.6, 30°C
1.05
2-hydroxy-2-methylpropanoyl-CoA
pH 6.6, 30°C, mutant enzyme D117A (mutation in subunit HcmA)
1.053
2-hydroxy-2-methylpropanoyl-CoA
mutant D117A, pH 6.6, 30°C
0.028
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme I90V (mutation in subunit HcmA)
0.062
isovaleryl-CoA
pH 6.6, 30°C, mutant enzyme D117V (mutation in subunit HcmA)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 7
pH 6.2: about 60% of maximal activity, pH 7.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 35
25°C: about 50% pf maxim al activity, 35°C: about 45% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
I3VE77 i.e. large subunit HcmA, I3VE74 i.e. small subunit HcmB
SwissProt
brenda
I3VE77, i.e. large subunit HcmA, I3VE74, i.e. small subunit HcmB, respectively
SwissProt
brenda
I3VE77: large subunit hcmA, I3VE74: small subunit hcmB
SwissProt
brenda
I3VE77 i.e. large subunit HcmA, I3VE74 i.e. small subunit HcmB
SwissProt
brenda
I3VE77: large subunit hcmA, I3VE74: small subunit hcmB
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
D5WTR7; D5WTR8
mutase from strain DSM 2912 catalyzes isomerization of (R)-3-hydroxybutanoyl-CoA about 7000 times more efficiently than the mutase from Aquincola tertiaricarbonis L108. The most striking structural difference between the two mutases, likely determining stereospecificity, is a replacement of active-site residue Asp found in strain L108 at position 117 with Val in the enzyme from strain DSM 2912, resulting in a reversed polarity at this binding site