BRENDA - Enzyme Database
show all sequences of 1.3.1.31

An enoate reductase Achr-OYE4 from Achromobacter sp. JA81: characterization and application in asymmetric bioreduction of CC bonds

Wang, H.; Pei, X.; Wu, Z.; Appl. Microbiol. Biotechnol. 98, 705-15 (2013) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli
Achromobacter sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
0.0191
-
NADH
pH 7.5, 30°C
Achromobacter sp.
0.0854
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40600
-
calculated from cDNA
Achromobacter sp.
45000
-
SDS-PAGE
Achromobacter sp.
Organism
Organism
UniProt
Commentary
Textmining
Achromobacter sp.
I3V5V6
-
-
Achromobacter sp. JA81
I3V5V6
-
-
Purification (Commentary)
Purification (Commentary)
Organism
using affinity chromatography
Achromobacter sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-methyl-N-phenylmaleimide + NADH + H+
-
724100
Achromobacter sp.
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
-
-
-
?
2-methyl-N-phenylmaleimide + NADH + H+
-
724100
Achromobacter sp. JA81
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
-
-
-
?
2-methyl-N-phenylmaleimide + NADPH
-
724100
Achromobacter sp.
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
-
-
-
?
2-methyl-N-phenylmaleimide + NADPH
-
724100
Achromobacter sp. JA81
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
Achr-OYE4
-
Achromobacter sp.
enoate reductase
-
Achromobacter sp.
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
optimal temperature in Tris-HCl buffer
Achromobacter sp.
35
-
optimal temperature in potassium phosphate buffer
Achromobacter sp.
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
-
about 40% of maximal activity maintained
Achromobacter sp.
45
-
about 40% of maximal activity maintained
Achromobacter sp.
55
-
no activity beyond 55°C
Achromobacter sp.
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
half-life of inactivation: 64.8 h
Achromobacter sp.
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.9
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
19.2
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
38.6
-
NADH
pH 7.5, 30°C
Achromobacter sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
highest activity using Tris-HCl
Achromobacter sp.
pH Range
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
no activity at pH 11
Achromobacter sp.
9
-
only 30% of highest activity at pH 9
Achromobacter sp.
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
-
Achromobacter sp.
NADH
preferred cofactor
Achromobacter sp.
NADPH
-
Achromobacter sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli
Achromobacter sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
-
Achromobacter sp.
NADH
preferred cofactor
Achromobacter sp.
NADPH
-
Achromobacter sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0014
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
0.0191
-
NADH
pH 7.5, 30°C
Achromobacter sp.
0.0854
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40600
-
calculated from cDNA
Achromobacter sp.
45000
-
SDS-PAGE
Achromobacter sp.
Purification (Commentary) (protein specific)
Commentary
Organism
using affinity chromatography
Achromobacter sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-methyl-N-phenylmaleimide + NADH + H+
-
724100
Achromobacter sp.
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
-
-
-
?
2-methyl-N-phenylmaleimide + NADH + H+
-
724100
Achromobacter sp. JA81
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NAD+
-
-
-
?
2-methyl-N-phenylmaleimide + NADPH
-
724100
Achromobacter sp.
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
-
-
-
?
2-methyl-N-phenylmaleimide + NADPH
-
724100
Achromobacter sp. JA81
(3R)-3-methyl-1-phenylpyrrolidine-2,5-dione + NADP+
-
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
optimal temperature in Tris-HCl buffer
Achromobacter sp.
35
-
optimal temperature in potassium phosphate buffer
Achromobacter sp.
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
20
-
about 40% of maximal activity maintained
Achromobacter sp.
45
-
about 40% of maximal activity maintained
Achromobacter sp.
55
-
no activity beyond 55°C
Achromobacter sp.
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
30
-
half-life of inactivation: 64.8 h
Achromobacter sp.
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.9
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
19.2
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
38.6
-
NADH
pH 7.5, 30°C
Achromobacter sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
highest activity using Tris-HCl
Achromobacter sp.
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
additional information
-
no activity at pH 11
Achromobacter sp.
9
-
only 30% of highest activity at pH 9
Achromobacter sp.
kcat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
4.4
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
220
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
2000
-
NADH
pH 7.5, 30°C
Achromobacter sp.
kcat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
4.4
-
2-methyl-N-phenylmaleimide
pH 7.5, 30°C
Achromobacter sp.
220
-
NADPH
pH 7.5, 30°C
Achromobacter sp.
2000
-
NADH
pH 7.5, 30°C
Achromobacter sp.
Other publictions for EC 1.3.1.31
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Protein Variants
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
Synonyms
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)
740123
Peters
Fusion proteins of an enoate r ...
Pseudomonas putida
Biol. Chem.
398
31-37
2017
-
-
-
-
-
-
-
-
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5
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4
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-
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-
740951
Sun
Aerobic biosynthesis of hydroc ...
Clostridium acetobutylicum
Metab. Eng.
35
75-82
2016
-
-
1
-
-
-
-
-
-
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-
4
-
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2
-
1
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1
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1
1
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2
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-
-
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-
728964
Gall
Enzymatic conversion of flavon ...
Eubacterium ramulus
Angew. Chem. Int. Ed. Engl.
53
1439-1442
2014
-
-
1
-
-
-
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2
1
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4
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2
2
2
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1
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2
2
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-
-
-
-
-
-
-
-
-
-
724100
Wang
An enoate reductase Achr-OYE4 ...
Achromobacter sp., Achromobacter sp. JA81
Appl. Microbiol. Biotechnol.
98
705-15
2013
-
-
1
-
-
-
-
3
-
-
2
-
-
9
-
-
1
-
-
-
-
-
4
-
2
2
3
1
3
1
2
-
3
-
-
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-
1
3
-
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-
-
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3
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-
2
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-
-
1
-
-
-
-
4
-
2
3
1
3
1
2
-
-
-
-
-
-
3
3
724734
Romagnolo
-
Fungal laccases and enoate red ...
Absidia glauca, Penicillium citrinum
Chem. Eng. Technol.
32
961-966
2013
-
-
-
-
-
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2
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1
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1
-
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-
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-
-
-
-
-
-
-
-
-
-
739971
Skrobiszewski
-
Pleurotus ostreatus as a sourc ...
Pleurotus ostreatus, Pleurotus ostreatus PO310783
Biocatal. Agricult. Biotechnol.
2
26-31
2013
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
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-
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12
-
1
-
-
-
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-
-
1
-
-
-
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-
1
-
-
-
-
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-
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-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
740318
Classen
-
Revisiting the enantioselectiv ...
Solanum lycopersicum, Photorhabdus luminescens
ChemCatChem
5
711-713
2013
-
-
1
-
-
-
-
-
-
-
2
-
-
2
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1
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10
2
3
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2
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1
2
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-
-
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-
2
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1
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-
10
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
741094
Paul
Mimicking nature: Synthetic ni ...
Thermus scotoductus
Org. Lett.
15
180-183
2013
-
-
-
-
-
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-
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1
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8
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1
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2
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2
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8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
724073
Liu
Asymmetric bioreduction of act ...
Achromobacter sp.
Appl. Microbiol. Biotechnol.
95
635-645
2012
-
-
1
-
-
-
-
-
-
-
-
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-
7
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-
-
-
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7
-
2
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3
-
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1
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-
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-
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-
7
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
724878
Gao
Biochemical characterization a ...
Lacticaseibacillus casei
Enzyme Microb. Technol.
51
26-34
2012
-
-
1
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-
2
-
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3
-
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5
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1
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16
1
2
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1
1
2
-
1
-
1
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1
1
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2
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3
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1
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16
1
-
1
1
2
-
1
-
-
-
-
-
-
-
-
726510
Iqbal
Asymmetric bioreduction of act ...
Shewanella sp.
Tetrahedron
68
7619-7623
2012
-
-
1
-
-
-
-
-
-
-
-
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4
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-
-
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16
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3
1
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1
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1
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-
-
16
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
724053
Richter
Asymmetric reduction of activa ...
Gluconobacter oxydans
Appl. Microbiol. Biotechnol.
89
79-89
2011
-
-
1
-
-
-
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2
-
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2
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4
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1
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6
-
1
4
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2
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2
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3
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1
3
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2
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2
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1
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6
-
4
-
2
-
2
-
-
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-
-
-
-
-
-
684248
Chaparro-Riggers
-
Comparison of three enoate red ...
Yersinia bercovieri, Kluyveromyces lactis, Pseudomonas putida
Adv. Synth. Catal.
349
1521-1531
2007
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3
-
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2
1
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-
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3
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3
-
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3
-
39
-
10
-
-
3
1
1
1
1
6
-
-
-
-
-
3
6
-
-
-
-
2
-
1
-
-
-
-
-
-
-
3
-
-
3
-
39
-
-
-
3
1
1
1
1
-
-
-
-
-
-
-
686271
Stuermer
Asymmetric bioreduction of act ...
Saccharomyces cerevisiae, Burkholderia sp., Marchantia polymorpha, Rhodotorula sp., Rhodotorula
Curr. Opin. Chem. Biol.
11
203-213
2007
-
-
-
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5
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7
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5
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5
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5
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7
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-
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-
-
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-
-
-
-
689312
Stueckler
Stereocomplementary bioreducti ...
Bacillus subtilis, Solanum lycopersicum
Org. Lett.
9
5409-5411
2007
-
-
2
-
-
-
5
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
12
-
3
-
-
-
-
-
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-
2
-
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-
2
2
-
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5
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12
-
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-
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-
-
-
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-
-
-
-
657039
de Kraker
Biosynthesis of costunolide, d ...
Cichorium intybus
Plant Physiol.
129
257-268
2002
3
-
-
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2
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2
-
2
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1
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3
-
1
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1
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3
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1
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2
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2
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1
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3
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390686
Rohdich
Enoate reductases of Clostridi ...
Clostridium tyrobutyricum, Moorella thermoacetica
J. Biol. Chem.
276
5779-5787
2001
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1
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390685
Caldeira
EPR and Moessbauer spectroscop ...
Clostridium tyrobutyricum
J. Biol. Chem.
271
18743-18748
1996
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4
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1
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390671
Verhaert
Enzyme kinetics in reversed mi ...
Clostridium sp.
Eur. J. Biochem.
187
73-79
1990
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2
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2
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390669
Preiss
-
Additional enoates amd other a ...
Clostridium tyrobutyricum
DECHEMA Biotechnol. Conf.
3
189-192
1989
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8
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1
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14
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3
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3
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8
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14
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390670
Krause
Design and application of sens ...
Clostridium sporogenes, Moorella thermoacetica, Clostridium tyrobutyricum
Z. Naturforsch. C
44
345-352
1989
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11
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3
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3
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3
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390672
Thanos
Reductions of 2-enals, dehydro ...
Clostridium kluyveri, Clostridium tyrobutyricum
Biol. Chem. Hoppe-Seyler
369
451-460
1988
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8
1
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4
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4
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390673
Thanos
-
Electroenzymatic and electromi ...
Clostridium tyrobutyricum
Methods Enzymol.
136
302-317
1987
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1
5
7
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1
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1
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1
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9
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1
1
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1
4
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1
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1
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5
4
7
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1
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1
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9
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1
1
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390674
Thanos
-
Electro-enzymic viologen-media ...
Clostridium tyrobutyricum
J. Biotechnol.
6
13-29
1987
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1
1
1
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1
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3
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1
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1
1
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3
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390675
Kuno
Structure of enoate reductase ...
Clostridium tyrobutyricum
Biol. Chem. Hoppe-Seyler
366
463-472
1985
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1
4
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9
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1
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1
1
1
2
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1
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1
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4
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1
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1
1
1
2
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390676
Bader
-
ATP formation is coupled to th ...
Clostridium sporogenes
FEMS Microbiol. Lett.
20
171-175
1983
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2
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390677
Giesel
On the occurrence of enoate re ...
Paraclostridium bifermentans, Clostridium botulinum, Clostridioides difficile, Paeniclostridium ghonii, Tissierella praeacuta, Clostridioides mangenotii, Clostridium oceanicum, Paeniclostridium sordellii, Clostridium sporogenes, Acetoanaerobium sticklandii, no activity in Clostridium butyricum, no activity in Clostridium pasteurianum, no activity in Clostridium propionicum, Peptostreptococcus anaerobius
Arch. Microbiol.
135
51-57
1983
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37
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33
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11
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11
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33
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390678
Giesel
-
Immunological relationship of ...
Clostridium kluyveri, Clostridium sp., Clostridium sporogenes, Clostridium tyrobutyricum
FEMS Microbiol. Lett.
19
43-45
1983
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4
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390679
Buehler
On the kinetics and mechanism ...
Clostridium kluyveri, Clostridium sp.
Hoppe-Seyler's Z. Physiol. Chem.
363
609-625
1982
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16
2
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6
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2
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31
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2
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2
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2
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16
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2
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31
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2
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390680
Egerer
Rhein as an electron acceptor ...
Clostridium sp.
Hoppe-Seyler's Z. Physiol. Chem.
363
627-633
1982
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1
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3
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390681
Bader
The reduction of allyl alcohol ...
Clostridium kluyveri, Clostridium sp.
Hoppe-Seyler's Z. Physiol. Chem.
362
809-820
1981
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2
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10
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6
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2
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6
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390682
Bader
The activities of hydrogenase ...
Clostridium kluyveri, Clostridium sp.
Arch. Microbiol.
127
279-287
1980
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4
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390683
Buehler
Occurrence and the possible ph ...
Clostridium kluyveri, Clostridium sp., Clostridium sporogenes, Peptostreptococcus anaerobius
FEBS Lett.
109
244-246
1980
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4
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10
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4
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10
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390684
Tischer
Purification and some properti ...
Clostridium kluyveri, Clostridium sp.
Eur. J. Biochem.
97
103-112
1979
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3
5
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1
2
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2
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1
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1
1
13
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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5
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1
2
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1
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1
1
13
1
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1
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1
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