BRENDA - Enzyme Database
show all sequences of 1.1.1.320

Stereoselective reduction of aromatic ketones by a new ketoreductase from Pichia glucozyma

Contente, M.L.; Serra, I.; Brambilla, M.; Eberini, I.; Gianazza, E.; De Vitis, V.; Molinari, F.; Zambelli, P.; Romano, D.; Appl. Microbiol. Biotechnol. 100, 193-201 (2016)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.64
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Ogataea glucozyma
A0A0H4SN47
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-(2-fluorophenyl)ethanone + NADPH + H+
76% of the rate with 1-(4-nitrophenyl)ethanone, 97% yield, 94% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(2-fluorophenyl)ethanol + NADP+
-
-
-
?
1-(2-nitrophenyl)ethanone + NADPH + H+
53% of the rate with 1-(4-nitrophenyl)ethanone, 78% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(2-nitrophenyl)ethanol + NADP+
-
-
-
?
1-(3-fluorophenyl)ethanone + NADPH + H+
61% of the rate with 1-(4-nitrophenyl)ethanone, 85% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(3-fluorophenyl)ethanol + NADP+
-
-
-
?
1-(4-nitrophenyl)ethanone + NADPH + H+
100% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(4-nitrophenyl)ethanol + NADP+
-
-
-
?
1-(furan-2-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(1S)-1-(furan-2-yl)ethanol + NADP+
48% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(pyridin-3-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(S)-(1-pyridin-3yl)ethanol + NADP+
58% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(pyridin-3-yl)propan-1-one + NADPH + H+
-
739919
Ogataea glucozyma
(S)-1-(pyridin-3-yl)propanol + NADP+
60% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(thiophen-2-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(1S)-1-(thiophen-2-yl)ethanol + NADP+
51% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
2-acetylbenzonitrile + NADPH + H+
82% of the rate with 1-(4-nitrophenyl)ethanone, 98% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
2-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
-
-
-
?
3-oxo-3-phenylpropanenitrile + NADPH + H+
-
739919
Ogataea glucozyma
(3S)-3-hydroxy-3-phenylpropanenitrile + NADP+
55% of the activity with benzil, 95% yield, 95% enantiomeric excess
-
-
?
4-acetylbenzonitrile + NADPH + H+
68% of the rate with 1-(4-nitrophenyl)ethanone, 70% yield, 97% enantiomeric excess
739919
Ogataea glucozyma
4-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
-
-
-
?
benzil + NADPH + H+
-
739919
Ogataea glucozyma
(S)-benzoin + NADP+
98% enantiomeric excess
-
-
?
benzophenone + NADPH + H+
-
739919
Ogataea glucozyma
diphenylmethanol + NADP+
66% yield
-
-
?
ethyl 2-oxo-2-phenylacetate + NADPH + H+
-
739919
Ogataea glucozyma
ethyl (2S)-hydroxy(phenyl)acetate + NADP+
115% yield, 40% enantiomeric excess
-
-
?
additional information
for the enantioselective reduction of mono-substituted acetophenones, reaction rates of meta- and para-derivatives are consistent with the electronic effects described by delta-Hammett coefficients. Enantioselectivity is determined by an opposite orientation of the substrate in the binding pocket. Reduction of ortho-derivatives occurs only with substrates bearing substituents with low steric impact, and reactivity is controlled by stereoelectronic features
739919
Ogataea glucozyma
?
-
-
-
-
additional information
the enzyme prefers space-demanding substrates, which are often converted with high stereoselectivity
739919
Ogataea glucozyma
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
35
-
Ogataea glucozyma
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
stable up to
Ogataea glucozyma
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.14
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Ogataea glucozyma
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
6
-
90% of maximum activity
Ogataea glucozyma
8
-
90% of maximum activity
Ogataea glucozyma
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.64
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-(2-fluorophenyl)ethanone + NADPH + H+
76% of the rate with 1-(4-nitrophenyl)ethanone, 97% yield, 94% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(2-fluorophenyl)ethanol + NADP+
-
-
-
?
1-(2-nitrophenyl)ethanone + NADPH + H+
53% of the rate with 1-(4-nitrophenyl)ethanone, 78% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(2-nitrophenyl)ethanol + NADP+
-
-
-
?
1-(3-fluorophenyl)ethanone + NADPH + H+
61% of the rate with 1-(4-nitrophenyl)ethanone, 85% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(3-fluorophenyl)ethanol + NADP+
-
-
-
?
1-(4-nitrophenyl)ethanone + NADPH + H+
100% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
(1S)-1-(4-nitrophenyl)ethanol + NADP+
-
-
-
?
1-(furan-2-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(1S)-1-(furan-2-yl)ethanol + NADP+
48% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(pyridin-3-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(S)-(1-pyridin-3yl)ethanol + NADP+
58% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(pyridin-3-yl)propan-1-one + NADPH + H+
-
739919
Ogataea glucozyma
(S)-1-(pyridin-3-yl)propanol + NADP+
60% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
1-(thiophen-2-yl)ethanone + NADPH + H+
-
739919
Ogataea glucozyma
(1S)-1-(thiophen-2-yl)ethanol + NADP+
51% of the activity with benzil, 95% yield, 98% enantiomeric excess
-
-
?
2-acetylbenzonitrile + NADPH + H+
82% of the rate with 1-(4-nitrophenyl)ethanone, 98% yield, 98% enantiomeric excess
739919
Ogataea glucozyma
2-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
-
-
-
?
3-oxo-3-phenylpropanenitrile + NADPH + H+
-
739919
Ogataea glucozyma
(3S)-3-hydroxy-3-phenylpropanenitrile + NADP+
55% of the activity with benzil, 95% yield, 95% enantiomeric excess
-
-
?
4-acetylbenzonitrile + NADPH + H+
68% of the rate with 1-(4-nitrophenyl)ethanone, 70% yield, 97% enantiomeric excess
739919
Ogataea glucozyma
4-[(1S)-1-hydroxyethyl]benzonitrile + NADP+
-
-
-
?
benzil + NADPH + H+
-
739919
Ogataea glucozyma
(S)-benzoin + NADP+
98% enantiomeric excess
-
-
?
benzophenone + NADPH + H+
-
739919
Ogataea glucozyma
diphenylmethanol + NADP+
66% yield
-
-
?
ethyl 2-oxo-2-phenylacetate + NADPH + H+
-
739919
Ogataea glucozyma
ethyl (2S)-hydroxy(phenyl)acetate + NADP+
115% yield, 40% enantiomeric excess
-
-
?
additional information
for the enantioselective reduction of mono-substituted acetophenones, reaction rates of meta- and para-derivatives are consistent with the electronic effects described by delta-Hammett coefficients. Enantioselectivity is determined by an opposite orientation of the substrate in the binding pocket. Reduction of ortho-derivatives occurs only with substrates bearing substituents with low steric impact, and reactivity is controlled by stereoelectronic features
739919
Ogataea glucozyma
?
-
-
-
-
additional information
the enzyme prefers space-demanding substrates, which are often converted with high stereoselectivity
739919
Ogataea glucozyma
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
35
-
Ogataea glucozyma
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
stable up to
Ogataea glucozyma
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.14
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8
-
Ogataea glucozyma
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
6
-
90% of maximum activity
Ogataea glucozyma
8
-
90% of maximum activity
Ogataea glucozyma
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.22
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.22
-
benzil
pH 8.0, 30°C
Ogataea glucozyma
Other publictions for EC 1.1.1.320
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739919
Contente
Stereoselective reduction of a ...
Ogataea glucozyma
Appl. Microbiol. Biotechnol.
100
193-201
2016
-
-
-
-
-
-
-
1
-
-
-
-
-
3
-
-
-
-
-
-
-
-
16
-
1
-
1
1
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
16
-
1
-
1
1
1
-
2
-
-
-
-
-
1
1
717892
Maruyama
The enzymes with benzil reduct ...
Bacillus cereus
J. Biotechnol.
94
157-169
2002
-
1
1
-
-
-
-
2
-
-
-
1
-
6
-
-
1
-
-
-
-
-
8
-
1
-
-
2
2
-
-
2
-
-
-
-
1
1
2
-
-
-
-
-
-
2
-
-
-
1
-
-
-
1
-
-
-
-
8
-
1
-
-
2
2
-
-
-
-
2
2
-
2
2
717406
Maruyama
Isolation and expression of a ...
Bacillus cereus, Bacillus cereus Tim-r01
Biotechnol. Bioeng.
75
630-633
2001
-
-
1
-
-
-
-
-
-
-
-
2
-
7
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-