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show all sequences of 1.1.1.B3

Purification and characterization of a novel NADH-dependent carbonyl reductase from Pichia stipitis involved in biosynthesis of optically pure ethyl (S)-4-chloro-3-hydroxybutanoate

Cao, H.; Mi, L.; Ye, Q.; Zang, G.; Yan, M.; Wang, Y.; Zhang, Y.; Li, X.; Xu, L.; Xiong, J.; Ouyang, P.; Ying, H.; Biores. Technol. 102, 1733-1739 (2011)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate in Escherichia coli. Coexpression of carbonyl reductase CRII and a glucose dehydrogenase gives an activity of 15 U/mg protein using ethyl 4-chloro-3-oxobutanoate as a substrate in a water/butyl acetate system. The transformants give a molar yield of 91%, and an optical purity of the (S)-isomer of more than 99% enantiomeric excess
Scheffersomyces stipitis
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Scheffersomyces stipitis
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
5 mM, 50% residual activity
Scheffersomyces stipitis
phenyl methyl sulfonylfluoride
5 mM, 49% residual activity
Scheffersomyces stipitis
sodium dodecylsulfate
1%, 51% residual activity
Scheffersomyces stipitis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.3
-
ethyl 4-chloro-3-oxobutanoate
pH 6.0, 30°C
Scheffersomyces stipitis
Organic Solvent Stability
Organic Solvent
Commentary
Organism
dimethyl formamide
1%, 56% residual activity
Scheffersomyces stipitis
dimethyl sulfoxide
1%, 67% residual activity
Scheffersomyces stipitis
tetrahydrofuran
1%, 77% residual activity
Scheffersomyces stipitis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Scheffersomyces stipitis
A3GF05
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme
Scheffersomyces stipitis
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
224
-
pH 6.0, 30°C
Scheffersomyces stipitis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-butanedione + NADH + H+
9% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
? + NAD+
-
-
-
?
2,3-pentanedione + NADH + H+
82% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
? + NAD+
-
-
-
?
ethyl 2-chloro-3-oxobutanoate + NADH + H+
49% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
ethyl 2-chloro-3-hydroxybutanoate + NAD+
-
-
-
?
ethyl 3-oxobutanoate + NADH + H+
28% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
ethyl 3-hydroxybutanoate + NAD+
-
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
-
724568
Scheffersomyces stipitis
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD+
product in more than 99% enantiomeric excess
-
-
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Scheffersomyces stipitis
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
35
more than 80% of maximum activity within
Scheffersomyces stipitis
50
-
no residual activity
Scheffersomyces stipitis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Scheffersomyces stipitis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5.5
7
more than 80% of maximum activity within
Scheffersomyces stipitis
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
5.6
-
between pH 5.6-7.0, 4°C, stable for 48 h
Scheffersomyces stipitis
7
-
between pH 5.6-7.0, 4°C, stable for 48 h
Scheffersomyces stipitis
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
preferred over NADPH
Scheffersomyces stipitis
NADPH
about 10% of the activity with NADH
Scheffersomyces stipitis
Application (protein specific)
Application
Commentary
Organism
synthesis
synthesis of ethyl (S)-4-chloro-3-hydroxybutanoate in Escherichia coli. Coexpression of carbonyl reductase CRII and a glucose dehydrogenase gives an activity of 15 U/mg protein using ethyl 4-chloro-3-oxobutanoate as a substrate in a water/butyl acetate system. The transformants give a molar yield of 91%, and an optical purity of the (S)-isomer of more than 99% enantiomeric excess
Scheffersomyces stipitis
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Scheffersomyces stipitis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
preferred over NADPH
Scheffersomyces stipitis
NADPH
about 10% of the activity with NADH
Scheffersomyces stipitis
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
5 mM, 50% residual activity
Scheffersomyces stipitis
phenyl methyl sulfonylfluoride
5 mM, 49% residual activity
Scheffersomyces stipitis
sodium dodecylsulfate
1%, 51% residual activity
Scheffersomyces stipitis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.3
-
ethyl 4-chloro-3-oxobutanoate
pH 6.0, 30°C
Scheffersomyces stipitis
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
dimethyl formamide
1%, 56% residual activity
Scheffersomyces stipitis
dimethyl sulfoxide
1%, 67% residual activity
Scheffersomyces stipitis
tetrahydrofuran
1%, 77% residual activity
Scheffersomyces stipitis
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Scheffersomyces stipitis
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
224
-
pH 6.0, 30°C
Scheffersomyces stipitis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,3-butanedione + NADH + H+
9% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
? + NAD+
-
-
-
?
2,3-pentanedione + NADH + H+
82% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
? + NAD+
-
-
-
?
ethyl 2-chloro-3-oxobutanoate + NADH + H+
49% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
ethyl 2-chloro-3-hydroxybutanoate + NAD+
-
-
-
?
ethyl 3-oxobutanoate + NADH + H+
28% of the activity with ethyl 4-chloro-3-oxobutanoate
724568
Scheffersomyces stipitis
ethyl 3-hydroxybutanoate + NAD+
-
-
-
?
ethyl 4-chloro-3-oxobutanoate + NADH + H+
-
724568
Scheffersomyces stipitis
ethyl (S)-4-chloro-3-hydroxybutanoate + NAD+
product in more than 99% enantiomeric excess
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
-
Scheffersomyces stipitis
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
35
more than 80% of maximum activity within
Scheffersomyces stipitis
50
-
no residual activity
Scheffersomyces stipitis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
-
Scheffersomyces stipitis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5.5
7
more than 80% of maximum activity within
Scheffersomyces stipitis
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
5.6
-
between pH 5.6-7.0, 4°C, stable for 48 h
Scheffersomyces stipitis
7
-
between pH 5.6-7.0, 4°C, stable for 48 h
Scheffersomyces stipitis
Other publictions for EC 1.1.1.B3
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)
724568
Cao
Purification and characterizat ...
Scheffersomyces stipitis
Biores. Technol.
102
1733-1739
2011
-
1
1
-
-
-
3
1
-
-
-
-
3
1
-
-
1
-
-
-
1
-
5
-
1
2
-
-
1
1
2
2
-
-
-
-
1
1
2
-
-
-
-
3
-
1
-
-
-
-
3
-
-
1
-
-
1
-
5
-
1
2
-
-
1
1
2
-
-
-
-
-
-
-
723841
Protsko
Crystallization and preliminar ...
Thermoanaerobacter ethanolicus
Acta Crystallogr. Sect. F
66
831-833
2010
-
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725726
Li
-
Deracemization of aryl seconda ...
Rhodotorula sp., Rhodotorula sp. AS2.2241
J. Mol. Catal. B
64
48-52
2010
-
1
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697267
Pal
Activity of yeast alcohol dehy ...
Saccharomyces carlsbergensis, Saccharomyces carlsbergensis Y379-50, Saccharomyces cerevisiae
Chem. Biol. Interact.
178
16-23
2009
-
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697839
Pennacchio
Role of Tryptophan 95 in subst ...
Sulfolobus solfataricus
Extremophiles
13
751-761
2009
-
-
1
1
1
-
-
4
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
4
-
-
-
1
-
-
-
-
-
1
1
1
1
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
701031
Rocha-Martin
-
Purification, immobilization a ...
Thermus thermophilus
Process Biochem.
44
1004-1012
2009
-
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
-
-
1
-
2
1
1
-
3
-
1
-
1
2
-
-
-
-
1
1
2
-
1
-
-
-
-
-
-
-
1
1
-
-
-
1
-
-
1
-
2
1
1
-
3
-
1
-
1
-
-
-
-
-
-
-
684583
Pennacchio
Purification and characterizat ...
Thermus thermophilus
Appl. Environ. Microbiol.
74
3949-3958
2008
1
1
1
-
-
-
7
6
-
5
4
-
1
5
-
-
1
-
-
-
1
-
7
1
2
1
4
5
2
2
-
3
-
-
-
1
1
1
3
-
-
-
-
7
-
6
-
5
4
-
1
-
-
1
-
-
1
-
7
1
2
1
4
5
2
2
-
-
-
-
-
-
-
-
689823
Soni
-
Purification and characterizat ...
Candida viswanathii, Candida viswanathii MTCC 5158
Process Biochem.
42
1632-1640
2007
1
-
-
-
-
-
30
2
-
-
2
-
7
3
-
-
1
-
-
-
1
1
14
1
1
2
1
-
1
1
-
2
-
-
-
1
-
-
2
-
-
-
-
30
-
2
-
-
2
-
7
-
-
1
-
-
1
1
14
1
1
2
1
-
1
1
-
-
-
-
-
-
-
-
685078
Hoeffken
Crystal structure and enzyme k ...
uncultured bacterium, uncultured bacterium EbN1
Biochemistry
45
82-93
2006
-
-
1
1
-
-
3
3
-
-
3
-
-
2
-
-
1
-
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
3
-
3
-
-
3
-
-
-
-
1
-
-
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684588
Abokitse
Cloning, sequence analysis, an ...
Rhodococcus erythropolis
Appl. Microbiol. Biotechnol.
62
380-386
2003
-
-
1
-
-
-
-
-
-
1
2
-
-
1
-
-
1
-
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
2
-
-
-
-
1
-
-
1
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685641
Yamamoto
-
Synthesis of (R)-1,3-butanedio ...
Candida parapsilosis
Biosci. Biotechnol. Biochem.
4
925-927
2002
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685644
Yamamoto
Synthesis of ethyl (R)-4-chlor ...
Candida parapsilosis
Biosci. Biotechnol. Biochem.
66
481-483
2002
-
1
1
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685643
Xie
NAD+-Dependent (S)-specific se ...
Nocardia fusca AKU 2123
Biosci. Biotechnol. Biochem.
63
1721-1729
1999
-
-
-
-
-
-
7
3
-
-
2
-
-
4
-
-
1
-
-
-
1
-
24
1
2
-
2
-
-
2
1
3
-
-
-
-
-
-
3
-
-
-
-
7
-
3
-
-
2
-
-
-
-
1
-
-
1
-
24
1
2
-
2
-
-
2
1
-
-
-
-
-
-
-