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show all sequences of 1.1.1.B3

Purification and characterization of a novel recombinant highly enantioselective short-chain NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus

Pennacchio, A.; Pucci, B.; Secundo, F.; La Cara, F.; Rossi, M.; Raia, C.A.; Appl. Environ. Microbiol. 74, 3949-3958 (2008)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
o-phenanthroline
activates to 108% activity compared to the control activity at 0.1 mM and to 109% at 1 mM
Thermus thermophilus
Application
Application
Commentary
Organism
synthesis
the enzyme is useful in production of chiral compounds for organic synthesis
Thermus thermophilus
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli strain BL21(DE3)
Thermus thermophilus
Inhibitors
Inhibitors
Commentary
Organism
Structure
1-butyl-3-methylimidazolium tetrafluoroborate
65% inhibition at 2 mM
Thermus thermophilus
Ca2+
10% inhibition at 1 mM and 30% at 100 mM
Thermus thermophilus
Cu2+
23% inhibition at 1 mM
Thermus thermophilus
Hg2+
67% inhibition at 1 mM
Thermus thermophilus
iodoacetate
5% inhibition at 1 mM
Thermus thermophilus
Mg2+
33% inhibition at 100 mM
Thermus thermophilus
additional information
no effects by 5 mM 2-mercaptoethanol
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and substrate specificity, overview
Thermus thermophilus
4.2
-
(S)-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.1
-
rac-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.3
-
rac-alpha-tetralol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.8
-
alpha-tetralone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
27.6
-
1-Indanone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
EDTA
activates to 127% activity compared to the control activity at 1 mM and to 163% at 10 mM
Thermus thermophilus
K+
activates to 167% activity compared to the control activity at 1 mM and to 193% at 100 mM
Thermus thermophilus
Li+
activates to 127% activity compared to the control activity at 1 mM and to 178% at 100 mM
Thermus thermophilus
Na+
activates to 179 at 100 mM
Thermus thermophilus
Zn2+
activates to 114% activity compared to the control activity at 1 mM
Thermus thermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
26961
-
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
71000
-
about, recombinant enzyme, gel filtration in absence of NaCl
Thermus thermophilus
105000
-
about, recombinant enzyme, gel filtration in presence of 0.15 M NaCl
Thermus thermophilus
Organic Solvent Stability
Organic Solvent
Commentary
Organism
additional information
the enzyme shows a good tolerance to common organic solvents
Thermus thermophilus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Thermus thermophilus
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant enzyme 11fold to homogeneity from Escherichia coli strain BL21(DE3) by heat denaturation of host proteins, anion exchange chromatography and gel filtration
Thermus thermophilus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
151.1
-
substrate: (S)-1-phenylethanol
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-phenylethanol + NAD+
99% ethanoselective reaction
684583
Thermus thermophilus
1 phenylethanone + NADH + H+
-
-
-
r
(S)-alpha-tetralol + NAD+
99% ethanoselective reaction
684583
Thermus thermophilus
alpha-tetralone + NADH + H+
-
-
-
r
1-indanone + NADH + H+
-
684583
Thermus thermophilus
(S)-1-indanol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
?
-
-
-
r
acetophenone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
(S)-1-phenylethanol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
r
alpha-tetralone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
(S)-alpha-tetralol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
r
additional information
substrate specificity of ADHTt in the oxidation and the reduction reactions depends on the substrate, cf. (R)-specific secondary alcohol dehydrogenase, detailed overview. The enzyme shows a high reduction rate with halogenated aryl ketones, such as 2,2,2-trifluoroacetophenone, 2-chloroacetophenone, and 4-chlorobutyrophenone, and with aryl diketones, such as 1-phenyl-1,2-propanedione, although it is not active on benzil, i.e. diphenylethanedione. ADHTt proves to be very effective in reducing aryl alpha-keto esters, although it is not active on aliphatic alpha-keto esters and aryl beta-keto ester. Critical role of the D37 residue in discriminating NAD(H) from NADP(H)
684583
Thermus thermophilus
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
oxidation reaction
Thermus thermophilus
65
-
reduction reaction
Thermus thermophilus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
73
the enzyme displays activity at temperatures up to 73°C
Thermus thermophilus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
24 h, purified recombinant enzyme, 142% inactivation
Thermus thermophilus
60
-
24 h, purified recombinant enzyme, 134% inactivation
Thermus thermophilus
70
-
24 h, purified recombinant enzyme, 107% inactivation
Thermus thermophilus
90
-
30 min, purified recombinant enzyme, 50% inactivation
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.7
-
alpha-tetralone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
8.3
-
1-Indanone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
45.7
-
rac-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
48.1
-
rac-alpha-tetralol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
61.4
-
(S)-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction reaction
Thermus thermophilus
10
-
oxidation reaction
Thermus thermophilus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
6
7.7
reduction reaction, high activity
Thermus thermophilus
9
10
oxidation reaction, high activity
Thermus thermophilus
Cofactor
Cofactor
Commentary
Organism
Structure
additional information
the enzyme shows no activity with NADP(H)
Thermus thermophilus
NAD+
critical role of the D37 residue in discriminating NAD(H) from NADP(H)
Thermus thermophilus
NADH
critical role of the D37 residue in discriminating NAD(H) from NADP(H)
Thermus thermophilus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
o-phenanthroline
activates to 108% activity compared to the control activity at 0.1 mM and to 109% at 1 mM
Thermus thermophilus
Application (protein specific)
Application
Commentary
Organism
synthesis
the enzyme is useful in production of chiral compounds for organic synthesis
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli strain BL21(DE3)
Thermus thermophilus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
additional information
the enzyme shows no activity with NADP(H)
Thermus thermophilus
NAD+
critical role of the D37 residue in discriminating NAD(H) from NADP(H)
Thermus thermophilus
NADH
critical role of the D37 residue in discriminating NAD(H) from NADP(H)
Thermus thermophilus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1-butyl-3-methylimidazolium tetrafluoroborate
65% inhibition at 2 mM
Thermus thermophilus
Ca2+
10% inhibition at 1 mM and 30% at 100 mM
Thermus thermophilus
Cu2+
23% inhibition at 1 mM
Thermus thermophilus
Hg2+
67% inhibition at 1 mM
Thermus thermophilus
iodoacetate
5% inhibition at 1 mM
Thermus thermophilus
Mg2+
33% inhibition at 100 mM
Thermus thermophilus
additional information
no effects by 5 mM 2-mercaptoethanol
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics and substrate specificity, overview
Thermus thermophilus
4.2
-
(S)-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.1
-
rac-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.3
-
rac-alpha-tetralol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
5.8
-
alpha-tetralone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
27.6
-
1-Indanone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
EDTA
activates to 127% activity compared to the control activity at 1 mM and to 163% at 10 mM
Thermus thermophilus
K+
activates to 167% activity compared to the control activity at 1 mM and to 193% at 100 mM
Thermus thermophilus
Li+
activates to 127% activity compared to the control activity at 1 mM and to 178% at 100 mM
Thermus thermophilus
Na+
activates to 179 at 100 mM
Thermus thermophilus
Zn2+
activates to 114% activity compared to the control activity at 1 mM
Thermus thermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
26000
-
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
26961
-
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
71000
-
about, recombinant enzyme, gel filtration in absence of NaCl
Thermus thermophilus
105000
-
about, recombinant enzyme, gel filtration in presence of 0.15 M NaCl
Thermus thermophilus
Organic Solvent Stability (protein specific)
Organic Solvent
Commentary
Organism
additional information
the enzyme shows a good tolerance to common organic solvents
Thermus thermophilus
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme 11fold to homogeneity from Escherichia coli strain BL21(DE3) by heat denaturation of host proteins, anion exchange chromatography and gel filtration
Thermus thermophilus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
151.1
-
substrate: (S)-1-phenylethanol
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-1-phenylethanol + NAD+
99% ethanoselective reaction
684583
Thermus thermophilus
1 phenylethanone + NADH + H+
-
-
-
r
(S)-alpha-tetralol + NAD+
99% ethanoselective reaction
684583
Thermus thermophilus
alpha-tetralone + NADH + H+
-
-
-
r
1-indanone + NADH + H+
-
684583
Thermus thermophilus
(S)-1-indanol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
?
2,2,2-trifluoroacetophenone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
?
-
-
-
r
acetophenone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
(S)-1-phenylethanol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
r
alpha-tetralone + NADH + H+
completely enantioselective reaction
684583
Thermus thermophilus
(S)-alpha-tetralol + NAD+
99% enantiomeric excess after 6 h at 50°C
-
-
r
additional information
substrate specificity of ADHTt in the oxidation and the reduction reactions depends on the substrate, cf. (R)-specific secondary alcohol dehydrogenase, detailed overview. The enzyme shows a high reduction rate with halogenated aryl ketones, such as 2,2,2-trifluoroacetophenone, 2-chloroacetophenone, and 4-chlorobutyrophenone, and with aryl diketones, such as 1-phenyl-1,2-propanedione, although it is not active on benzil, i.e. diphenylethanedione. ADHTt proves to be very effective in reducing aryl alpha-keto esters, although it is not active on aliphatic alpha-keto esters and aryl beta-keto ester. Critical role of the D37 residue in discriminating NAD(H) from NADP(H)
684583
Thermus thermophilus
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 26961, recombinant enzyme, mass spectrometry, 4 * 26000, recombinant enzyme, SDS-PAGE
Thermus thermophilus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
oxidation reaction
Thermus thermophilus
65
-
reduction reaction
Thermus thermophilus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
73
the enzyme displays activity at temperatures up to 73°C
Thermus thermophilus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
24 h, purified recombinant enzyme, 142% inactivation
Thermus thermophilus
60
-
24 h, purified recombinant enzyme, 134% inactivation
Thermus thermophilus
70
-
24 h, purified recombinant enzyme, 107% inactivation
Thermus thermophilus
90
-
30 min, purified recombinant enzyme, 50% inactivation
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
7.7
-
alpha-tetralone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
8.3
-
1-Indanone
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
45.7
-
rac-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
48.1
-
rac-alpha-tetralol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
61.4
-
(S)-1-indanol
pH 6.0, 65°C, recombinant enzyme, reduction reaction
Thermus thermophilus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
reduction reaction
Thermus thermophilus
10
-
oxidation reaction
Thermus thermophilus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
6
7.7
reduction reaction, high activity
Thermus thermophilus
9
10
oxidation reaction, high activity
Thermus thermophilus
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
-
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4
1
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1
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1
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3
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3
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3
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1
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4
1
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1
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1
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5
1
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1
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1
2
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1
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1
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5
1
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1
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-
-
-
-
-
-
1
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-
-
-
-
2
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-
-
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1
1
2
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-
-
-
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-
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-
-
-
1
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-
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-
-
-
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1
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1
1
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1
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7
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1
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1
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24
1
2
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2
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2
1
3
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3
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7
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3
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2
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1
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1
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24
1
2
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2
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2
1
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