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(E)-2-oxo-4(pyridin-3-yl)-3-butenoic acid
3-(pyridin-3-yl)acrylaldehyde + CO2
-
-
-
?
(p-methoxybenzoyl)formate
p-methoxybenzaldehyde + CO2
-
-
-
-
?
(p-methylbenzoyl)formate
p-methylbenzaldehyde + CO2
(R)-2-hydroxy-1-phenylpropanone + acetaldehyde
?
-
-
-
-
r
(S)-2-hydroxy-1-phenylpropanone + acetaldehyde
?
-
-
-
-
r
2 benzaldehyde
(R)-benzoin
2-fluoro-benzaldehyde + acetaldehyde
(S)-1-(2-fluoro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
2-fluoro-benzaldehyde + acetaldehyde
1-(2-fluoro-phenyl)-2-hydroxy-propan-1-one
-
91% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
2-fluorobenzaldehyde
(R)-1,2-Bis-(2-fluoro-phenyl)-2-hydroxy-ethanone
-
carboligation
68% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
2-furaldehyde
(R)-1,2-di-furan-2-yl-2-hydroxy-ethanone
-
carboligation
62% yield and 94% enantiomeric excess of the (R)-enantiomer
-
?
2-furaldehyde + acetaldehyde
(S)-1-Furan-2-yl-2-hydroxy-propan-1-one
-
-
-
-
?
2-ketohexanoate
valeraldehyde + CO2
-
-
-
?
2-ketopentanoate
butyraldehyde + CO2
-
-
-
?
2-methyl-benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-(2-methylphenyl)-propanone
-
-
-
-
?
2-methyl-benzaldehyde + acetaldehyde
2-hydroxy-1-o-tolyl-propan-1-one
-
4% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
2-oxo-3-phenylpropanoic acid
phenylacetaldehyde + CO2
-
-
-
?
2-oxo-4-methylhexanoic acid
3-methylpentanal + CO2
-
-
-
?
2-oxo-4-methylpentanoic acid
3-methylbutanal + CO2
-
-
-
?
2-oxo-4-phenylbutanoic acid
3-phenylpropionaldehyde + CO2
-
-
-
?
2-oxo-5-phenylpentanoic acid
4-phenylpentanal + CO2
-
-
-
?
2-oxobutanoate
propionaldehyde + CO2
-
-
-
?
2-oxobutanoic acid
propionaldehyde + CO2
-
-
-
?
2-oxohexanoate
valeraldehyde + CO2
2-oxohexanoic acid
valeraldehyde + CO2
-
-
-
?
2-oxopentanoate
butyraldehyde + CO2
-
-
-
?
2-oxopentanoic acid
butyraldehyde + CO2
-
-
-
?
3 benzaldehyde + acetaldehyde
(R)-benzoin + (S)-2-hydroxypropiophenone
-
-
-
?
3,5-Difluoro-benzaldehyde + acetaldehyde
(S)-1-(3,5-Difluoro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3,5-dimethoxybenzaldehyde + acetaldehyde
(S)-1-(3,5-Dimethoxy-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3-Benzyloxy-benzaldehyde + acetaldehyde
1-(3-Benzyloxy-phenyl)-2-hydroxy-propan-1-one
-
more than 99% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-bromo-benzaldehyde + acetaldehyde
(S)-1-(3-bromo-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3-bromo-benzaldehyde + acetaldehyde
1-(3-bromo-phenyl)-2-hydroxy-propan-1-one
-
96% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-chloro-benzaldehyde + acetaldehyde
(S)-1-(3-chloro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3-chloro-benzaldehyde + acetaldehyde
1-(3-chloro-phenyl)-2-hydroxy-propan-1-one
-
94% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-ethoxy-4-hydroxybenzoylformate
ethyl vanillin + CO2
3-ethoxy-benzaldehyde + acetaldehyde
(S)-1-(3-ethoxy-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3-ethoxy-benzaldehyde + acetaldehyde
1-(3-ethoxy-phenyl)-2-hydroxy-propan-1-one
-
97% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-fluoro-benzaldehyde + acetaldehyde
(S)-1-(3-fluoro-phenyl)-2-hydroxy-propan-1-one
3-formyl-benzonitrile + acetaldehyde
3-((S)-2-hydroxy-propionyl)-benzonitrile
-
-
-
-
?
3-formyl-benzonitrile + acetaldehyde
3-(2-hydroxy-propionyl)-benzonitrile
-
92% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-hydroxy-benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-(3-hydroxy-phenyl)-propan-1-one
-
-
-
-
?
3-hydroxy-benzaldehyde + acetaldehyde
2-hydroxy-1-(3-hydroxy-phenyl)-propan-1-one
-
92% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-isopropoxy-benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-(3-isopropoxy-phenyl)-propan-1-one
-
-
-
-
?
3-isopropoxy-benzaldehyde + acetaldehyde
2-hydroxy-1-(3-isopropoxy-phenyl)-propan-1-one
-
more thahn 99% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-methoxy-benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-(3-methoxy-phenyl)-propan-1-one
-
-
-
-
?
3-methoxy-benzaldehyde + acetaldehyde
2-hydroxy-1-(3-methoxy-phenyl)-propan-1-one
-
96% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-methoxybenzaldehyde
(R)-2-Hydroxy-1,2-bis-(3-methoxy-phenyl)-ethanone
-
carboligation
18% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
3-Methoxymethoxy-benzaldehyde + acetaldehyde
(S)-2-Hydroxy-1-(3-methoxymethoxy-phenyl)-propan-1-one
-
-
-
-
?
3-methyl-2-oxobutanoate
2-methylpropanal + CO2
-
-
-
?
3-methyl-2-oxobutanoic acid
2-methylpropanal + CO2
-
-
-
?
3-methyl-2-oxopentanoate
2-methylbutanal + CO2
-
-
-
?
3-methyl-2-oxopentanoic acid
2-methylbutanal + CO2
-
-
-
?
3-methyl-benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-m-tolyl-propan-1-one
-
-
-
-
?
3-methyl-benzaldehyde + acetaldehyde
2-hydroxy-1-m-tolyl-propan-1-one
-
97% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
3-Phenoxy-benzaldehyde + acetaldehyde
2-Hydroxy-1-(3-phenoxy-phenyl)-propan-1-one
-
more than 99% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4,4-dimethyl-2-oxopentanoic acid
3,3-dimethylbutanal + CO2
-
-
-
?
4-Bromo-benzaldehyde + acetaldehyde
1-(4-Bromo-phenyl)-2-hydroxy-propan-1-one
-
83% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-bromobenzaldehyde
(R)-1,2-bis-(4-bromo-phenyl)-2-hydroxy-ethanone
-
carboligation
13% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
4-bromobenzaldehyde + acetaldehyde
(S)-1-(4-Bromo-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
4-Chloro-benzaldehyde + acetaldehyde
1-(4-Chloro-phenyl)-2-hydroxy-propan-1-one
-
82% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-chlorobenzaldehyde
(R)-1,2-bis-(4-chloro-phenyl)-2-hydroxy-ethanone
-
carboligation
17% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
4-chlorobenzaldehyde + acetaldehyde
(S)-1-(4-Chloro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
4-fluoro-benzaldehyde + acetaldehyde
(S)-1-(4-fluoro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
4-fluoro-benzaldehyde + acetaldehyde
1-(4-fluoro-phenyl)-2-hydroxy-propan-1-one
-
87% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-fluorobenzaldehyde
(R)-1,2-Bis-(4-fluoro-phenyl)-2-hydroxy-ethanone
-
carboligation
25% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
4-Formyl-benzonitrile + acetaldehyde
4-(2-Hydroxy-propionyl)-benzonitrile
-
74% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-formylbenzonitrile + acetaldehyde
4-((S)-2-Hydroxy-propionyl)-benzonitrile
-
-
-
-
?
4-Hydroxy-benzaldehyde + acetaldehyde
2-Hydroxy-1-(4-hydroxy-phenyl)-propan-1-one
-
86% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-hydroxybenzaldehyde + acetaldehyde
(S)-2-Hydroxy-1-(4-hydroxy-phenyl)-propan-1-one
-
-
-
-
?
4-Methoxy-benzaldehyde + acetaldehyde
2-Hydroxy-1-(4-methoxy-phenyl)-propan-1-one
-
92% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-methoxybenzaldehyde
(R)-2-Hydroxy-1,2-bis-(4-methoxy-phenyl)-ethanone
-
carboligation
12% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
4-methoxybenzaldehyde + acetaldehyde
(S)-2-Hydroxy-1-(4-methoxy-phenyl)-propan-1-one
-
-
-
-
?
4-methyl-2-oxopentanoate
3-methylbutanal + CO2
-
-
-
?
4-Methyl-benzaldehyde + acetaldehyde
2-Hydroxy-1-p-tolyl-propan-1-one
-
88% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-methylbenzaldehyde
(R)-2-Hydroxy-1,2-di-p-tolyl-ethanone
-
carboligation
69% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
4-methylbenzaldehyde + acetaldehyde
(S)-2-Hydroxy-1-p-tolyl-propan-1-one
-
-
-
-
?
4-methylthio-2-oxobutanoate
3-(methylsulfanyl)propanal + CO2
5-Isopropyl-furan-2-carbaldehyde + acetaldehyde
2-Hydroxy-1-(5-isopropyl-furan-2-yl)-propan-1-one
-
73% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
5-methyl-furan-2-carbaldehyde
(R)-2-Hydroxy-1,2-bis-(5-methyl-furan-2-yl)-ethanone
-
carboligation
50% yield and 96% enantiomeric excess of the (R)-enantiomer
-
?
5-Methyl-furan-2-carbaldehyde + acetaldehyde
2-Hydroxy-1-(5-methyl-furan-2-yl)-propan-1-one
-
86% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
8-Hydroxy-quinoline-2-carbaldehyde + acetaldehyde
2-Hydroxy-1-(8-hydroxy-quinolin-2-yl)-propan-1-one
-
-
-
-
?
acetaldehyde
(R)-acetoin
-
-
-
-
?
acetaldehyde + acetaldehyde
(3R)-3-hydroxybutan-2-one
-
-
-
-
?
acetic acid 3-formyl-phenyl ester + acetaldehyde
(S)-1-(3-acetoxyphenyl)-2-hydroxy-propanone
-
-
-
-
?
acetic acid 3-formyl-phenyl ester + acetaldehyde
acetic acid 3-(2-hydroxy-propionyl)-phenyl ester
-
more than 99% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
benzaldehyde + acetaldehyde
(R)-2-hydroxypropiophenone
-
reactions performed at high benzaldehyde concentrations and at high hydrostatic pressures show an increase in (R)-2-hydroxypropiophenone ((R)-2-HPP) formation catalyzed by BFD variants F464I, A460I, and A460I/F464I. For BFD mutant A460I/F464I there is an increase in the ee of (R)-2-HPP up to 80%, whereas at atmospheric conditions this variant synthesizes (R)-2-HPP with an ee of only 50%. Alkaline conditions (up to pH 8.5) and high hydrostatic pressures result in an increase of (R)-2-HPP synthesis, especially in the case of variant A460I and F464I
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-phenyl-propanone
benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-phenylpropan-1-one
-
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-phenylpropanone
-
-
-
-
r
benzaldehyde + acetaldehyde
(S)-2-hydroxypropiophenone
benzaldehyde + acetaldehyde
2-hydroxy-1-phenyl-propan-1-one
-
92% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
benzaldehyde + acetaldehyde
2-hydroxypropiophenone
benzaldehyde + benzaldehyde
(2R)-2-hydroxy-1,2-diphenylethanone
-
-
-
-
?
benzaldehyde + benzaldehyde
(R)-benzoin
benzoin + acetaldehyde
2-hydroxy-1-phenylpropanone
-
-
-
-
r
benzoylformate
benzaldehyde + CO2
Benzoylformate + acetaldehyde
(S)-2-Hydroxypropiophenone
benzylformate
benzaldehyde + CO2
cyclohex-1-ene-1-carbaldehyde + acetaldehyde
(S)-1-Cyclohex-1-enyl-2-hydroxy-propan-1-one
-
-
-
-
?
Cyclohex-1-enecarbaldehyde + acetaldehyde
1-Cyclohex-1-enyl-2-hydroxy-propan-1-one
-
94% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
cyclohexanecarbaldehyde + acetaldehyde
(S)-1-cyclohexyl-2-hydroxy-propan-1-one
-
-
-
-
?
cyclohexanecarbaldehyde + acetaldehyde
1-cyclohexyl-2-hydroxy-propan-1-one
-
61% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
Furan-2-carbaldehyde + acetaldehyde
1-Furan-2-yl-2-hydroxy-propan-1-one
-
45% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
isovaleraldehyde
(R)-5-hydroxy-2,7-dimethyloctan-4-one
-
-
-
-
?
m-bromo-benzoylformate
m-bromo-benzaldehyde + CO2
wild-type enzyme: 68% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 97% conversion with more than 98% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 98.5% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
m-chloro-benzoylformate
m-chloro-benzaldehyde + CO2
wild-type enzyme: 94% conversion with 94% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
m-fluoro-benzoylformate
m-fluoro-benzaldehyde + CO2
wild-type enzyme: 100% conversion with 87% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 94% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
m-methoxy-benzoylformate
m-methoxy-benzaldehyde + CO2
wild-type enzyme: 94% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
m-methyl-benzoylformate
m-methyl-benzaldehyde + CO2
wild-type enzyme: 99% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
methyl benzoylphosphonate
?
-
-
-
?
n-butanal
(R)-5-hydroxyoctan-4-one
-
-
-
-
?
n-pentanal
(R)-6-hydroxydecan-5-one
-
-
-
-
?
Naphthalene-2-carbaldehyde + acetaldehyde
2-Hydroxy-1-naphthalen-2-yl-propan-1-one
-
-
-
-
?
nicotinaldehyde + acetaldehyde
(S)-2-Hydroxy-1-pyridin-3-yl-propan-1-one
-
-
-
-
?
o-bromo-benzoylformate
o-bromo-benzaldehyde + CO2
wild-type enzyme: no activity, mutant enzyme L476Q: 98% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 90% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
o-chloro-benzoylformate
o-chloro-benzaldehyde + CO2
wild-type enzyme: no activity, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 85% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
o-fluoro-benzoylformate
o-fluoro-benzaldehyde + CO2
wild-type enzyme: 91% conversion with 89% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 83% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
o-methoxy-benzoylformate
o-methoxy-benzaldehyde + CO2
wild-type enzyme: no conversion, mutant enzyme L476Q: 97% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 46% conversion with 99% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
o-methyl-benzoylformate
o-methyl-benzaldehyde + CO2
wild-type enzyme: 4% conversion, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 83% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
o-methylbenzaldehyde + acetaldehyde
(2S)-2-hydroxy-1-(2-methylphenyl)propan-1-one
mutant enzyme L476Q and M365L/L461S selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme
-
-
?
p-bromo-benzoylformate
p-bromo-benzaldehyde + CO2
wild-type enzyme: 42% conversion with 83% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with 96.5% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 96% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
p-chloro-benzoylformate
p-chloro-benzaldehyde + CO2
wild-type enzyme: 85% conversion with 82% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 96.5% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 100% conversion with 95.5% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
p-fluoro-benzoylformate
p-fluoro-benzaldehyde + CO2
wild-type enzyme: 69% conversion with 87% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 87% conversion with 97% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
p-methoxy-benzoylformate
p-methoxy-benzaldehyde + CO2
wild-type enzyme: 23% conversion with 92% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 99% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 67% conversion with 42% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
p-methyl-benzoylformate
p-methyl-benzaldehyde + CO2
wild-type enzyme: 65% conversion with 88% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme L476Q: 100% conversion with more than 98% enantiomeric excess of the (S)-2-hydroxy ketone, mutant enzyme M365L-L461S: 98% conversion with 98% enantiomeric excess of the (S)-2-hydroxy ketone
-
-
?
p-nitro-benzoylformate
?
very poor substrate
-
-
?
p-nitrobenzoylformate
p-nitrobenzaldehyde + CO2
-
-
-
-
?
phenylglyoxylate
benzaldehyde + CO2
Phenylpyruvate
Phenylacetaldehyde + CO2
-
-
-
?
propanal
4-hydroxyhexan-3-one
-
-
-
-
?
propionaldehyde
?
-
-
-
?
pyridine-2-carbaldehyde
(R)-2-Hydroxy-1,2-di-pyridin-2-yl-ethanone
-
carboligation
70% yield and 94% enantiomeric excess of the (R)-enantiomer
-
?
Pyridine-2-carbaldehyde + acetaldehyde
2-Hydroxy-1-pyridin-2-yl-propan-1-one
-
-
-
-
?
Pyridine-3-carbaldehyde + acetaldehyde
2-Hydroxy-1-pyridin-3-yl-propan-1-one
-
-
-
-
?
pyruvate
acetaldehyde + CO2
Quinoline-4-carbaldehyde + acetaldehyde
2-Hydroxy-1-quinolin-4-yl-propan-1-one
-
-
-
-
?
thiophene-2-carbaldehyde
(S)-2-Hydroxy-1,2-di-thiophen-2-yl-ethanone
-
carboligation
65% yield and 95% enantiomeric excess of the (R)-enantiomer
-
?
thiophene-2-carbaldehyde + acetaldehyde
(S)-2-hydroxy-1-thiophen-2-yl-propan-1-one
-
-
-
-
?
thiophene-2-carbaldehyde + acetaldehyde
2-hydroxy-1-thiophen-2-yl-propan-1-one
-
83% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
[m-(Fluoromethyl)benzoyl]formate
?
-
-
-
-
?
[p-(Chloromethyl)benzoyl]formate
?
-
-
-
-
?
[p-(Fluoromethyl)benzoyl]formate
?
-
-
-
-
?
additional information
?
-
(p-methylbenzoyl)formate
p-methylbenzaldehyde + CO2
-
-
-
?
(p-methylbenzoyl)formate
p-methylbenzaldehyde + CO2
-
-
-
-
?
2 benzaldehyde
(R)-benzoin
-
-
-
?
2 benzaldehyde
(R)-benzoin
-
-
-
-
?
2 benzaldehyde
(R)-benzoin
-
-
-
-
r
2 benzaldehyde
(R)-benzoin
-
-
i.e. (R)-2-hydroxy-1,2-diphenylethan-1-one
-
?
2-oxohexanoate
valeraldehyde + CO2
-
best substrate
-
-
?
2-oxohexanoate
valeraldehyde + CO2
-
best substrate
-
-
?
2-oxohexanoate
valeraldehyde + CO2
-
-
-
?
3-ethoxy-4-hydroxybenzoylformate
ethyl vanillin + CO2
-
-
-
?
3-ethoxy-4-hydroxybenzoylformate
ethyl vanillin + CO2
-
-
-
?
3-fluoro-benzaldehyde + acetaldehyde
(S)-1-(3-fluoro-phenyl)-2-hydroxy-propan-1-one
-
-
-
-
?
3-fluoro-benzaldehyde + acetaldehyde
(S)-1-(3-fluoro-phenyl)-2-hydroxy-propan-1-one
-
87% enantiomeric excess of the (S)-2-hydroxypropanone derivative
-
-
?
4-methylthio-2-oxobutanoate
3-(methylsulfanyl)propanal + CO2
-
-
-
-
?
4-methylthio-2-oxobutanoate
3-(methylsulfanyl)propanal + CO2
-
-
-
-
?
4-methylthio-2-oxobutanoate
3-(methylsulfanyl)propanal + CO2
-
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-phenyl-propanone
-
-
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxy-1-phenyl-propanone
-
the enantiomeric excess of (S)-2-hydroxy-1-phenyl-propanonedecreases with increasing temperature from 4°C to 30°C
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxypropiophenone
-
-
-
-
?
benzaldehyde + acetaldehyde
(S)-2-hydroxypropiophenone
-
-
-
r
benzaldehyde + acetaldehyde
(S)-2-hydroxypropiophenone
-
i.e. acyloin
-
?
benzaldehyde + acetaldehyde
2-hydroxypropiophenone
-
-
-
-
?
benzaldehyde + acetaldehyde
2-hydroxypropiophenone
-
-
-
?
benzaldehyde + benzaldehyde
(R)-benzoin
-
-
-
?
benzaldehyde + benzaldehyde
(R)-benzoin
-
-
-
-
?
benzaldehyde + benzaldehyde
(R)-benzoin
-
-
-
r
benzaldehyde + benzaldehyde
(R)-benzoin
-
carboligation
70% yield and more than 99% enantiomeric excess of the (R)-enantiomer
-
?
benzaldehyde + benzaldehyde
(R)-benzoin
-
in the liquid phase
-
-
?
Benzoylformate
?
-
enzyme is involved in the inducible pathway of mandelate
-
-
?
Benzoylformate
?
-
enzyme is involved in the metabolism of mandelic acid
-
-
?
Benzoylformate
?
-
enzyme is involved in the metabolism of mandelic acid
-
-
?
Benzoylformate
?
-
enzyme is involved in the inducible pathway of mandelate
-
-
?
Benzoylformate
?
-
enzyme is involved in the metabolism of mandelic acid
-
-
?
Benzoylformate
?
-
induced by mandelate
-
-
?
Benzoylformate
?
third enzyme in the mandelate pathway
-
-
?
Benzoylformate
?
-
enzyme is involved in the metabolic pathway of phenylglycine
-
-
?
Benzoylformate
?
-
enzyme is involved in the metabolic pathway of phenylglycine
-
-
?
Benzoylformate
?
-
induced by mandelate
-
-
?
Benzoylformate
?
-
the enzyme is involved in the pathway for catabolism of D(+)-mandelate and L-(-)-mandelate
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
655230, 677679, 678222, 678577, 679212, 679656, 680352, 680979, 682628, 715697, 716121 -
-
?
benzoylformate
benzaldehyde + CO2
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
highest activity
-
-
?
benzoylformate
benzaldehyde + CO2
best substrate for wild-type enzyme and mutant enzymes A460I, F464I, and A4670I, F464I
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
-
?
benzoylformate
benzaldehyde + CO2
-
-
-
?
Benzoylformate + acetaldehyde
(S)-2-Hydroxypropiophenone
-
-
-
-
?
Benzoylformate + acetaldehyde
(S)-2-Hydroxypropiophenone
-
-
-
?
Benzoylformate + acetaldehyde
(S)-2-Hydroxypropiophenone
-
-
benzaldehyde and benzyl alcohol are formed as by-products
?
benzylformate
benzaldehyde + CO2
-
-
-
-
?
benzylformate
benzaldehyde + CO2
-
-
-
?
phenylglyoxylate
benzaldehyde + CO2
-
-
-
-
?
phenylglyoxylate
benzaldehyde + CO2
-
-
-
-
ir
phenylglyoxylate
benzaldehyde + CO2
-
-
-
?
phenylglyoxylate
benzaldehyde + CO2
-
-
-
?
pyruvate
acetaldehyde + CO2
activity of wild-type enzyme is very low, very low activity with mutant enzymes A460I, F464I, and A4670I, F464I
-
-
?
pyruvate
acetaldehyde + CO2
pyruvate is no substrate for the wild type enzyme
-
-
?
additional information
?
-
-
very low activity with pyruvate, phenylpyruvate, 2-2oxopentanoate, 3-methyl-2-oxopentanoate, 2-oxobutanoate, and 3-methyl-2-oxobutanoate. No activity with 2-oxoglutarate
-
-
?
additional information
?
-
-
very low activity with pyruvate, phenylpyruvate, 2-2oxopentanoate, 3-methyl-2-oxopentanoate, 2-oxobutanoate, and 3-methyl-2-oxobutanoate. No activity with 2-oxoglutarate
-
-
?
additional information
?
-
-
best substrates in enantioselective synthesis of (S)-2-hydroxypropanone derivatives by C-C bond formation are meta-substituted benzaldehyde derivatives
-
-
?
additional information
?
-
no activity with 3,3-dimethyl-2-oxopentanoic acid and cyclohexaneglyoxylic acid (wild-type enzyme and mutant enzymes A460I, F464I and A460I/F464I)
-
-
?
additional information
?
-
-
no activity with 3,3-dimethyl-2-oxopentanoic acid and cyclohexaneglyoxylic acid (wild-type enzyme and mutant enzymes A460I, F464I and A460I/F464I)
-
-
?
additional information
?
-
does not perform the cleavage of 2-hydroxy ketones
-
-
?
additional information
?
-
-
does not perform the cleavage of 2-hydroxy ketones
-
-
?
additional information
?
-
-
isobutyraldehyde, pivalaldehyde, and tert-butylacetaldehyde are no substrates
-
-
?
additional information
?
-
the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives is not catalyzed by the wild type enzyme, but with mutant enzyme L461A
-
-
?
additional information
?
-
-
the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives is not catalyzed by the wild type enzyme, but with mutant enzyme L461A
-
-
?
additional information
?
-
-
the enzyme performs enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes
-
-
?
additional information
?
-
when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
-
-
?
additional information
?
-
-
when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
-
-
?
additional information
?
-
-
synthesis of (S)-2-hydroxy-1-phenylpropanone by the immobilized recombinant enzyme is effective in cross acyloin reaction of benzaldehyde with acetaldehyde. The immobilized and free enzymes shows similar substrate specificity and activity
-
-
?
additional information
?
-
-
the enzyme also performs the cross acyloin reaction of benzaldehyde with acetaldehyde to give (S)-2-hydroxy-1-phenylpropanone
-
-
?
additional information
?
-
-
the enzyme has the ability to carry out stereospecific carbon-carbon bond formation, with products including various 2-hydroxy ketones and benzoin derivatives, the enzyme also catalyzes the conversion of benzaldehyde and acetaldehyde into R-benzoin and, predominantly, S-2-hydroxypropiophenone, via stereospecific carboligation
-
-
?
additional information
?
-
the enzyme exhibits very limited activity with pyruvate
-
-
?
additional information
?
-
when 3-ethoxy-4-hydroxybenzoylformate is provided at with Pseudomonas putida, it is completely transformed to ethyl vanillic acid after 2 days, but only trace amounts of ethyl vanillin are detected. Similar results are obtained when ethyl vanillin replaces 3-ethoxy-4-hydroxybenzoylformate as substrate, thus aldehyde dehydrogenation activity in Pseudomonas putida is greater than its synthesis activity. The recombinant Escherichia coli strain expressing the enzyme from Pseudomonas putida converts (S)-3-ethoxy-4-hydroxymandelic acid into ethyl vanillin, but does not degrade ethyl vanillin, overview
-
-
?
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0.056
(p-methoxybenzoyl)formate
-
-
0.19 - 0.58
(p-methylbenzoyl)formate
62
(R)-2-hydroxy-1-phenylpropanone
-
at pH 7.5 and 30°C
62
(S)-2-hydroxy-1-phenylpropanone
-
at pH 7.5 and 30°C
0.42 - 7.5
2-ketobutanoate
0.15 - 4.1
2-ketohexanoate
1.1
2-oxo-4-methylhexanoic acid
pH 6.0, 30°C, mutant enzyme A460I
3.4 - 9.6
2-oxo-4-methylpentanoic acid
0.39 - 4.1
2-oxobutanoate
18.3
2-oxobutanoic acid
pH 6.0, 30°C, mutant enzyme A460I
1 - 4.1
2-oxohexanoic acid
0.15 - 11
2-oxopentanoate
1.2 - 6
2-oxopentanoic acid
0.77
3-methyl-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1.2
3-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.14 - 9.6
4-methyl-2-oxopentanoate
0.14 - 21
4-methylthio-2-oxobutanoate
0.059 - 15
benzoylformate
0.76
methyl benzoylphosphonate
-
0.15
p-nitro-benzoylformate
at 25°C
0.27 - 7.8
phenylglyoxylate
0.82
phenylpyruvate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.023
[m-(fluoromethyl)benzoyl]formate
-
-
0.021 - 0.18
[p-(Chloromethyl)benzoyl]formate
0.19
[p-(Fluoromethyl)benzoyl]formate
-
-
additional information
additional information
-
0.19
(p-methylbenzoyl)formate
-
-
0.58
(p-methylbenzoyl)formate
-
-
0.42
2-ketobutanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.3
2-ketobutanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.3
2-ketobutanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
7.5
2-ketobutanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.15
2-ketohexanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.28
2-ketohexanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.3
2-ketohexanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.1
2-ketohexanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.1
2-ketopentanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.28
2-ketopentanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.1
2-ketopentanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6
2-ketopentanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
3.4
2-oxo-4-methylpentanoic acid
pH 6.0, 30°C, mutant enzyme A460I
9.6
2-oxo-4-methylpentanoic acid
pH 6.0, 30°C, wild-type enzyme
0.39
2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
4.1
2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
0.14
2-Oxohexanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
5.3
2-Oxohexanoate
wild type enzyme, at pH 6.0 and 30°C
21
2-Oxohexanoate
-
wild type enzyme, at pH 6.0 and 30°C
1
2-oxohexanoic acid
pH 6.0, 30°C, mutant enzyme A460I
4.1
2-oxohexanoic acid
pH 6.0, 30°C, wild-type enzyme
0.15
2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
11
2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
1.2
2-oxopentanoic acid
pH 6.0, 30°C, mutant enzyme A460I
6
2-oxopentanoic acid
pH 6.0, 30°C, wild-type enzyme
0.14
4-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
9.6
4-methyl-2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
0.14
4-methylthio-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1.3
4-methylthio-2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
21
4-methylthio-2-oxobutanoate
-
wild type enzyme, at pH 6.0 and 30°C
310
acetaldehyde
-
pH 7.0
515.9
acetaldehyde
immobilized mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C
775
acetaldehyde
free mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C
19.4
benzaldehyde
free mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C
51.9
benzaldehyde
immobilized mutant enzyme A460I/F464I, in 50 mM phosphate buffer at pH 7.5 and 20°C
0.059
benzoylformate
-
-
0.06
benzoylformate
mutant enzyme L461V, in potassium phosphate buffer (pH 6.5, 50 mM)
0.2
benzoylformate
pH 6.0, 30°C, mutant enzyme A460I
0.2
benzoylformate
mutant enzyme A460I
0.23
benzoylformate
in 50 mM potassium phosphate buffer, pH 6.5, at 30°C
0.25
benzoylformate
mutant enzyme L461A, in potassium phosphate buffer (pH 6.5, 50 mM)
0.27
benzoylformate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.27
benzoylformate
wild type enzyme, at pH 6.0 and 30°C
0.29
benzoylformate
mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.29
benzoylformate
mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.37
benzoylformate
pH 7.0, wild-type enzyme
0.37
benzoylformate
wild type enzyme, in potassium phosphate buffer (pH 6.5, 50 mM)
0.38
benzoylformate
mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.4
benzoylformate
mutant enzyme H281A
0.44
benzoylformate
-
recombinant, his-tagged enzyme at pH 6.0 and 35°C
0.45
benzoylformate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.49
benzoylformate
mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.51
benzoylformate
mutant enzyme P24A, in potassium phosphate buffer (pH 6.5, 50 mM)
0.54
benzoylformate
wild-type enzyme
0.54
benzoylformate
-
wild type enzyme, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.54
benzoylformate
mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.58
benzoylformate
mutant enzyme L476Q
0.58
benzoylformate
-
mutant enzyme L476Q, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.59
benzoylformate
-
mutant enzyme L476G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.6
benzoylformate
-
mutant enzyme S181T/L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.69
benzoylformate
-
wild type enzyme at pH 6.0 and 35°C
0.8
benzoylformate
wild type enzyme
0.8
benzoylformate
pH 6.0, 30°C, wild-type enzyme
0.8
benzoylformate
mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.85
benzoylformate
mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.85
benzoylformate
mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.89
benzoylformate
mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.9
benzoylformate
mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.94
benzoylformate
mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1
benzoylformate
-
mutant enzyme L476H, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.02
benzoylformate
-
mutant enzyme L476T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.03
benzoylformate
-
mutant enzyme L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.06
benzoylformate
-
mutant enzyme L476Q/S525G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.08
benzoylformate
-
mutant enzyme L476M, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.1
benzoylformate
pH 6.0, 30°C, mutant enzyme A460I/F464I
1.1
benzoylformate
mutant enzyme A460I/F464I
1.14
benzoylformate
-
mutant enzyme L476S, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.17
benzoylformate
-
mutant enzyme L476A, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.2
benzoylformate
mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.2
benzoylformate
mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.23
benzoylformate
-
mutant enzyme S181T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.26
benzoylformate
-
mutant enzyme L476C, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.4
benzoylformate
mutant enzyme L461G, in potassium phosphate buffer (pH 6.5, 50 mM)
1.46
benzoylformate
-
mutant enzyme L476K, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.5
benzoylformate
mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.54
benzoylformate
mutant enzyme A460G, in potassium phosphate buffer (pH 6.5, 50 mM)
1.68
benzoylformate
pH 7.0, mutant enzyme H281A
1.9
benzoylformate
mutant enzyme H70A
1.92
benzoylformate
pH 7.0, mutant enzyme H70A
2 - 3
benzoylformate
-
wild type enzyme, at pH 6.0 and 30°C
2.3
benzoylformate
pH 6.0, 30°C, mutant enzyme F464I
2.3
benzoylformate
mutant enzyme F464I
2.9
benzoylformate
mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.5
benzoylformate
mutant enzyme S26A
7.8
benzoylformate
mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
8.62
benzoylformate
pH 7.0, mutant enzyme S26A
15
benzoylformate
-
mutant enzyme I466A, at pH 6.0 and 30°C
0.04
benzylformate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.27
benzylformate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.45
benzylformate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.5
benzylformate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.27
phenylglyoxylate
-
pH and temperature not specified in the publication, wild-type enzyme
0.38
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70L
0.49
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281Y
0.54
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281F
0.8
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26M
0.85
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70F
1.2
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281A
1.2
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26L
1.5
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70A
7.8
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26A
2
pyruvate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.8
pyruvate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
21
pyruvate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.021
[p-(Chloromethyl)benzoyl]formate
-
-
0.18
[p-(Chloromethyl)benzoyl]formate
-
-
additional information
additional information
KM-value of wild-type enzyme for 2-oxo-4-methylhexanoic acid (pH 6.0, 30°C) is above 20 mM
-
additional information
additional information
-
KM-value of wild-type enzyme for 2-oxo-4-methylhexanoic acid (pH 6.0, 30°C) is above 20 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.1 - 5.3
2-ketohexanoate
0.81 - 11
2-ketopentanoate
8.6 - 9.8
2-oxo-4-methylhexanoic acid
11 - 38
2-oxo-4-methylpentanoic acid
17.3 - 18.8
2-oxobutanoic acid
21 - 71.8
2-oxohexanoic acid
40.6 - 44.3
2-oxopentanoic acid
12
3-methyl-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
16
3-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
2.7 - 11
4-methyl-2-oxopentanoate
4.5 - 20
4-methylthio-2-oxobutanoate
0.07 - 1349
benzoylformate
0.05
p-nitro-benzoylformate
at 25°C
0.46 - 320
phenylglyoxylate
2
phenylpyruvate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
4
2-ketobutanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
5.8
2-ketobutanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6
2-ketobutanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
7.5
2-ketobutanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.1
2-ketohexanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.2
2-ketohexanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.4
2-ketohexanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
5.3
2-ketohexanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.81
2-ketopentanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
3.3
2-ketopentanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6.2
2-ketopentanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
11
2-ketopentanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
8.6
2-oxo-4-methylhexanoic acid
pH 6.0, 30°C, wild-type enzyme
9.8
2-oxo-4-methylhexanoic acid
pH 6.0, 30°C, mutant enzyme A460I
11
2-oxo-4-methylpentanoic acid
pH 6.0, 30°C, wild-type enzyme
38
2-oxo-4-methylpentanoic acid
pH 6.0, 30°C, mutant enzyme A460I
6
2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
7.5
2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
17.3
2-oxobutanoic acid
pH 6.0, 30°C, wild-type enzyme
18.8
2-oxobutanoic acid
pH 6.0, 30°C, mutant enzyme A460I
4.1
2-Oxohexanoate
wild type enzyme, at pH 6.0 and 30°C
5.9
2-Oxohexanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
20
2-Oxohexanoate
-
wild type enzyme, at pH 6.0 and 30°C
21
2-oxohexanoic acid
pH 6.0, 30°C, wild-type enzyme
71.8
2-oxohexanoic acid
pH 6.0, 30°C, mutant enzyme A460I
1.1
2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
6
2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
40.6
2-oxopentanoic acid
pH 6.0, 30°C, mutant enzyme A460I
44.3
2-oxopentanoic acid
pH 6.0, 30°C, wild-type enzyme
2.7
4-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
11
4-methyl-2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
4.5
4-methylthio-2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
4.6
4-methylthio-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
20
4-methylthio-2-oxobutanoate
-
wild type enzyme, at pH 6.0 and 30°C
0.07
benzoylformate
pH 7.0, mutant enzyme H70A
0.46
benzoylformate
mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.41
benzoylformate
pH 7.0, mutant enzyme H281A
2
benzoylformate
mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
2.1
benzoylformate
mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.45
benzoylformate
pH 7.0, mutant enzyme S26A
4.5
benzoylformate
mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.6
benzoylformate
-
mutant enzyme I466A, at pH 6.0 and 30°C
5.1
benzoylformate
-
wild type enzyme, at pH 6.0 and 30°C
5.6
benzoylformate
mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6.9
benzoylformate
mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
8.6
benzoylformate
mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
14
benzoylformate
mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
15
benzoylformate
mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
15
benzoylformate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
17
benzoylformate
mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
19
benzoylformate
mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
21
benzoylformate
pH 6.0, 30°C, mutant enzyme A460I/F464I
26
benzoylformate
mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
42
benzoylformate
mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
62
benzoylformate
pH 6.0, 30°C, mutant enzyme A460I
65
benzoylformate
mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
94
benzoylformate
mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
123
benzoylformate
pH 6.0, 30°C, mutant enzyme F464I
132
benzoylformate
mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
222
benzoylformate
-
wild type enzyme at pH 6.0 and 35°C
241
benzoylformate
pH 7.0, wild-type enzyme
284
benzoylformate
-
recombinant, his-tagged enzyme at pH 6.0 and 35°C
320
benzoylformate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
320
benzoylformate
wild type enzyme, at pH 6.0 and 30°C
426
benzoylformate
at 30°C, in 50 mM potassium phosphate buffer, pH 6.5
1349
benzoylformate
pH 6.0, 30°C, wild-type enzyme
1.7
benzylformate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
25
benzylformate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
110
benzylformate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
320
benzylformate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.46
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70A
2.1
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281A
4.5
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70F
6.9
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281Y
14
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70L
15
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26A
26
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26M
65
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281F
132
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26L
320
phenylglyoxylate
-
pH and temperature not specified in the publication, wild-type enzyme
1.4
pyruvate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
2
pyruvate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
3.6
pyruvate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.86 - 16
2-ketohexanoate
1.8 - 22
2-ketopentanoate
1.8 - 7.5
2-oxopentanoate
2.6 - 15
3-methyl-2-oxobutanoate
1.6 - 13
3-methyl-2-oxopentanoate
1.1 - 20
4-methyl-2-oxopentanoate
0.95 - 33
4-methylthio-2-oxobutanoate
0.22 - 1180
benzoylformate
0.3 - 1180
phenylglyoxylate
0.5
2-ketobutanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.7
2-ketobutanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.6
2-ketobutanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
14
2-ketobutanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.86
2-ketohexanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.3
2-ketohexanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
8
2-ketohexanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
16
2-ketohexanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.8
2-ketopentanoate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
3
2-ketopentanoate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
8.1
2-ketopentanoate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
22
2-ketopentanoate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.5
2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
16
2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.94
2-Oxohexanoate
-
wild type enzyme, at pH 6.0 and 30°C
1.3
2-Oxohexanoate
wild type enzyme, at pH 6.0 and 30°C
42
2-Oxohexanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1.8
2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
7.5
2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
2.6
3-methyl-2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
15
3-methyl-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1.6
3-methyl-2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
13
3-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1.1
4-methyl-2-oxopentanoate
wild type enzyme, at pH 6.0 and 30°C
20
4-methyl-2-oxopentanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.95
4-methylthio-2-oxobutanoate
-
wild type enzyme, at pH 6.0 and 30°C
3.5
4-methylthio-2-oxobutanoate
wild type enzyme, at pH 6.0 and 30°C
33
4-methylthio-2-oxobutanoate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.22
benzoylformate
-
wild type enzyme, at pH 6.0 and 30°C
0.3
benzoylformate
-
mutant enzyme I466A, at pH 6.0 and 30°C
34
benzoylformate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
1180
benzoylformate
wild type enzyme, at pH 6.0 and 30°C
16
benzylformate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
43
benzylformate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
244
benzylformate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1180
benzylformate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.3
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70A
1.7
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281A
1.9
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26A
5.3
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70F
14
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281Y
32
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26M
36
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H70L
110
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant S26L
120
phenylglyoxylate
-
pH and temperature not specified in the publication, mutant H281F
1180
phenylglyoxylate
-
pH and temperature not specified in the publication, wild-type enzyme
0.1
phenylpyruvate
wild type enzyme, at pH 6.0 and 30°C
2.5
phenylpyruvate
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.012
pyruvate
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.065
pyruvate
mutant enzyme A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.42
pyruvate
mutant enzyme T377L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.8
pyruvate
mutant enzyme T377L/A460Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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A460G
mutant exhibits a higher Km value compared to the wild type enzyme
G464I
activity with pyruvate is higher than wild-type activity, activity with 2-oxobutanoic acid is 1.2fold lower than wild-type activity, activity with 2-oxopentanoic acid is 4.8fold lower than wild-type value, activity with 2-oxohexanoic acid is 1.6fold lower than wild-type activity, activity with 3-methyl-2-oxobutanoic acid is 1.1fold higher than wild-type activity, activity with 3-methyl-2-oxopentanoic acid is 1.3fold higher than wild-type activity, activity with 2-oxo-4-methylpentanoic acid is 1.1fold higher than wild-type activity, activity with 4,4-dimethyl-2-oxopentanoic acid is identical to wild-type activity, activity with 2-oxo-4-methylhexanoic acid is 1.3fold higher than wild-type activity, activity with, activity with benzoylformate is 9.2fold lower than wild-type activity, activity with 2-oxo-3-phenylpropanoic acid is identical to wild-type activity, activity with 2-oxo-4-phenylbutanoic acid is9.3fold lower than wild-type activity, no activity with 2-oxo-5-phenylpentanoic acid. The ratio of turnover number to KM-value for benzoylformate is 31.8fold lower than the wild-type value. Mutation has no effect on the range of products obtained by carboligation of acetaldehyde and benzaldehyde, the yield of the product 2-hydroxypropiophenone an decreases about 3fold and the enantioselectivity of acetoin and 2-hydroxypropiophenone is altered
H281N
mutant with 17fold decrease in kcat value compared to the wild type enzyme
H281Q
mutant with 37fold decrease in kcat value compared to the wild type enzyme
H281T
mutant with 159fold decrease in kcat value compared to the wild type enzyme
H281W
mutant with 19fold decrease in kcat value compared to the wild type enzyme
H70S
mutant exhibits a 197fold decrease in kcat/Km compared to the wild type enzyme
L403E
-
kcat value of the L403E variant is only 18fold lower than that of wild-type BFDC
L403F
-
L403F variant shows about 10fold increased Km value for the substrate compared to the wild-type enzyme, the cofactor is displaced with the thiazolium ring away
L403X
-
half the L403X colonies screened have at least 10% of wild-type activity
L461V
mutant exhibits a higher Km value compared to the wild type enzyme
L476A
-
has a 4.11fold higher carboligase activity than the wild type enzyme
L476C
-
has a 4.31fold higher carboligase activity than the wild type enzyme
L476G
-
has a 4.27fold higher carboligase activity than the wild type enzyme
L476K
-
has a 5fold higher carboligase activity than the wild type enzyme
L476M
-
has a 4.23fold higher carboligase activity than the wild type enzyme
L476P/S181T
-
mutant with low cofactor binding affinity
L476Q/S535G
-
decreased activity
L476S
-
has a 3.5fold higher carboligase activity than the wild type enzyme
L476T
-
has a 3.98fold higher carboligase activity than the wild type enzyme
M365L/L461S
mutant enzyme selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme. Mutant enzyme retains only 9% of the wild-type BFD carboligase activity. Decrease in Vmax value as well as an increase in the Km-value for decarboxylation of benzoylformate by mutant enzyme compared to that of wild-type enzyme
P24A
mutant exhibits a higher Km value compared to the wild type enzyme
S181T/L476P
-
increased activity
S26T
mutant exhibits no significant loss of activity compared to the wild type enzyme (3fold decrease in kcat value)
I466A
-
the mutant shows increased catalytic efficiency for benzoylformate compared to the wild type enzyme
I466A
-
the mutant shows increased catalytic efficiency for benzoylformate compared to the wild type enzyme
-
A460I
strongly decreased activity
A460I
activity with pyruvate is higher than wild-type activity, activity with 2-oxobutanoic acid is 2.3fold higher than wild-type activity, activity with 2-oxopentanoic acid is 1.1fold lower than wild-type activity, activity with 2-oxohexanoic acid is 3.3fold higher than wild-type activity, activity with 3-methyl-2-oxobutanoic acid is 1.3fold higher than wild-type activity, activity with 3-methyl-2-oxopentanoic acid is 1.1fold lower than wild-type activity, activity with 2-oxo-4-methylpentanoic acid is 1.3fold higher than wild-type activity, activity with 4,4-dimethyl-2-oxopentanoic acid is identical to wild-type activity, activity with 2-oxo-4-methylhexanoic acid is 2.2fold higher than wild-type activity, activity with benzoylformate is 22.5fold lower than wild-type activity, activity with 2-oxo-3-phenylpropanoic acid is identical to wild-type activity, activity with 2-oxo-4-phenylbutanoic acid is 1.8fold higher than wild-type activity, activity with 2-oxo-5-phenylpentanoic acid is identical to wild-type activity. The ratio of turnover number to KM-value for 2-oxo-4-methylpentanoic acid is 10fold higher than the wild-type value, the ratio of turnover number to KM-value for 2-oxo-4-methylhexanoic acid is 1.13fold higher than the wild-type value, the ratio of turnover number to KM-value for benzoylformate is 5.4fold lower than the wild-type value, the ratio of turnover number to KM-value for 2-oxohexanoic acid is 14.1fold higher than the wild-type value, the ratio of turnover number to KM-value for 2-oxopentanoic acid is 4.6fold higher than the wild-type value. Mutation has no effect on the range of products obtained by carboligation of acetaldehyde and benzaldehyde, the yield of the product 2-hydroxypropiophenone an decreases about 3fold and the enantioselectivity of acetoin and 2-hydroxypropiophenone is altered
A460I
-
for this variant the highest amounts of (S)-2-hydroxypropiophenone-product can be detected at low benzaldehyde concentrations and slightly acidic conditions at pH 6.5
A460I
-
the mutant exhibits an increased (R)-2-hydroxypropiophenone selectivity
A460I
-
site-directed mutagenesis, the mutant enzymes is an excellent 2-ketohexanoate decarboxylase
A460I/F464I
strongly decreased activity
A460I/F464I
activity with pyruvate is higher than wild-type activity, activity with 2-oxobutanoic acid is 1.8fold lower than wild-type activity, activity with 2-oxopentanoic acid is 9.2fold lower than wild-type value, activity with 2-oxohexanoic acid is 3.3fold lower than wild-type activity, activity with 3-methyl-2-oxobutanoic acid is 1.5fold lower than wild-type activity, activity with 3-methyl-2-oxopentanoic acid is 1.2fold lower than wild-type activity, activity with 2-oxo-4-methylpentanoic acid is 1.5fold lower than wild-type activity, activity with 4,4-dimethyl-2-oxopentanoic acid is 10fold lower than wild-type activity, activity with 2-oxo-4-methylhexanoic acid is 1.1fold lower than wild-type activity, activity with benzoylformate is 64.3fold lower than wild-type activity, no activity with 2-oxo-3-phenylpropanoic acid, activity with 2-oxo-4-phenylbutanoic acid is 1.3fold lower than wild-type activity, activity with 2-oxo-5-phenylpentanoic acid is fold higher than wild-type activity. the ratio of turnover number to KM-value for benzoylformate is 88.7fold lower than the wild-type value
A460I/F464I
-
for this variant the highest amounts of (S)-2-hydroxypropiophenone-product can be detected at low benzaldehyde concentrations and slightly acidic conditions at pH 6.5
A460I/F464I
-
the mutant exhibits an increased (R)-2-hydroxypropiophenone selectivity
A460Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
A460Y
the mutant shows significantly improved catalytic activity toward pyruvate
F464I
strongly decreased activity
F464I
-
for this variant the highest amounts of (S)-2-hydroxypropiophenone-product can be detected at low benzaldehyde concentrations and slightly acidic conditions at pH 6.5
F464I
-
the mutant exhibits an increased (R)-2-hydroxypropiophenone selectivity
H281A
inactive
H281A
4.5fold increase in Km-value for benzoylformate, 3443fold decrease in turnover number for benzoylformate, 171fold increase in Ki-value for (R)-mandelate compared to wild-type enzyme
H281A
strongly decreased activity
H281A
mutant with 152fold decreased kcat value compared to the wild type enzyme
H281A
-
mutant with high cofactor binding affinity
H281A
-
site-directed mutagenesis, the mutant shows about 600fold reduced catalytic efficiency compared to the wild-type enzyme
H281F
mutant with 4.9fold decrease in kcat value compared to the wild type enzyme
H281F
the mutation leads to a 5fold decrease in the enzyme activity
H281F
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H281Y
mutant with 46fold decrease in kcat value compared to the wild type enzyme
H281Y
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H70A
inactive
H70A
5.2fold increase in Km-value for benzoylformate, 3443fold decrease in turnover number for benzoylformate, 40fold increase in Ki-value for (R)-mandelate compared to wild-type enzyme
H70A
strongly decreased activity
H70A
mutant exhibits 4000fold decreased catalytic activity compared to the wild type enzyme
H70A
-
site-directed mutagenesis, the mutant shows about 4000fold reduced catalytic efficiency compared to the wild-type enzyme
H70F
mutant exhibits a 236fold decrease in kcat/Km compared to the wild type enzyme
H70F
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H70L
mutant exhibits a 33fold decrease in kcat/Km compared to the wild type enzyme
H70L
the mutant shows 30% decrease in the enzyme activity
H70L
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H70T
mutant exhibits a 25fold decrease in kcat/Km compared to the wild type enzyme
H70T
the mutant shows 30% decrease in the enzyme activity
L461A
the mutant catalyzes the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives (a reaction not catalyzed by the wild type enzyme)
L461A
the mutant has decreased activity compared to the wild type enzyme, the enantioselectivity of the (S)-2-hydroxypropiophenone formation is increased by 6%. In the case of propionaldehyde, the enzyme activity increases considerably from 6% with wild type BFD to 21.5%. With butyraldehyde the already low enzyme activity does not change
L461G
the mutant catalyzes the S-stereoselective addition of larger acceptor aldehydes, such as propanal with benzaldehyde and its derivatives (a reaction not catalyzed by the wild type enzyme)
L461G
the mutant has decreased activity compared to the wild type enzyme, the enantioselectivity of the (S)-2-hydroxypropiophenone formation is increased by 6%. In the case of propionaldehyde, the enzyme activity increases considerably from 6% with wild type BFD to 23%. With butyraldehyde the already low enzyme activity does not change
L476H
-
has a 3.19fold higher carboligase activity than the wild type enzyme
L476H
-
mutant with low cofactor binding affinity
L476P
-
decreased activity
L476P
-
mutant with low cofactor binding affinity
L476P
-
the mutant variant shows improved carboligase activity in organic solvents compared to the wild-type enzyme
L476Q
mutant enzyme selectively catalyzes the formation of enantiopure (S)-2-hydroxy-1-(2-methylphenyl)propan-1-one with excellent yield, a reaction which is only poorly catalyzed by the wild-type enzyme. Vmax and Km-value for decraboxylation of benzoylformate are not effected
L476Q
-
has a 5.06fold higher carboligase activity than the wild type enzyme
L476Q
-
the mutant has an intermediate cofactor binding strength
L476Q
-
the mutant variant shows improved carboligase activity in organic solvents compared to the wild-type enzyme
S181T
-
has a 1.75fold higher carboligase activity than the wild type enzyme
S181T
-
mutant with high cofactor binding affinity
S26A
23.1fold increase in Km-value for benzoylformate, 54fold decrease in turnover number for benzoylformate, 100fold increase in Ki-value for (R)-mandelate compared to wild-type enzyme
S26A
strongly decreased activity
S26A
mutant with 21fold decrease in kcat value compared to the wild type enzyme
S26A
-
site-directed mutagenesis, the mutant shows about 600fold reduced catalytic efficiency compared to the wild-type enzyme, the S26A variant showed a 30fold increase in Km for benzoylformate and a 100fold increase in Ki value for R-mandelate
S26L
mutant exhibits no significant loss of activity compared to the wild type enzyme (2fold decrease in kcat value)
S26L
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
S26M
mutant exhibits no significant loss of activity compared to the wild type enzyme (12fold decrease in kcat value)
S26M
-
site-saturation mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T377L
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
T377L
the mutant shows significantly improved catalytic activity toward pyruvate
T377L/A460Y
-
site-directed mutagenesis, the mutant shows altered substrate specificity and kinetics compared to the wild-type enzyme
T377L/A460Y
the double mutant shows significantly improved catalytic activity toward pyruvate (11000fold improvement in the ratio between pyruvate and benzoylformate utilization)
T377L/A460Y
the mutant exhibits a greater than 10000fold increase in pyruvate/benzoylformate substrate utilization ratio compared to that of the wild type enzyme
additional information
biotransformation using recycled resting Escherichia coli cells expressing the enzyme, the product yield is above 42% after four repeated cycles
additional information
-
biotransformation using recycled resting Escherichia coli cells expressing the enzyme, the product yield is above 42% after four repeated cycles
additional information
-
covalent immobilization and stabilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic nanoparticles by a three-step immobilization/stabilization procedure at pH 8.0, 20°C, method development and evaluation, overview. The maximum enzyme loading is found to be 5.2 mg/g support in 3.5 mg/ml initial enzyme concentration at ionic strength of 1.25 M MgSO4. The covalently-bound enzyme is characterized in terms of its activity and stability for the formation of (S)-2-hydroxypropiophenone. The immobilized biocatalyst retains 95% of its original activity after five reaction cycles
additional information
-
immobilization of the purified recombinant His-tagged enzyme on magnetic nanoparticles, microspheres, nanospheres and ferrofluids, for enantioselective synthesis of (S)-2-hydroxyketones. Its stereoselectivity is highly dependent on the structure of the substrate aldehydes. Adsorption capacity of the Cu+2 charged magnetic solid support for His-tagged BFD is determined by standard BSA assay as 43.6 mg enzyme/g magnetic solid support
additional information
-
site-saturation mutagenesis is used to evolve stereoselective enzymes as catalysts for synthetic organic chemistry
additional information
-
biotransformation using recycled resting Escherichia coli cells expressing the enzyme, the product yield is above 42% after four repeated cycles
-
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Pseudomonas putida (P20906)
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Pseudomonas putida
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2016
Pseudomonas putida (P20906)
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27
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2015
Pseudomonas putida
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