BRENDA - Enzyme Database
show all sequences of 1.3.1.31

On the kinetics and mechanism of enoate reductase

Buehler, M.; Simon, H.; Hoppe-Seyler's Z. Physiol. Chem. 363, 609-625 (1982) View publication on PubMed

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
3-Phenylpropionate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
3-Phenylpropionate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
4-phenylbutanoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
4-phenylbutanoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
benzoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
benzoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
dicoumarol
blocks the NAD-binding domain
Clostridium kluyveri
dicoumarol
blocks the NAD-binding domain
Clostridium sp.
fumarate
-
Clostridium kluyveri
fumarate
-
Clostridium sp.
morin
blocks the NAD-binding domain
Clostridium kluyveri
morin
blocks the NAD-binding domain
Clostridium sp.
NAD+
mixed-type inhibitor
Clostridium kluyveri
NAD+
mixed-type inhibitor
Clostridium sp.
phenylacetate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
phenylacetate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Clostridium kluyveri
additional information
-
additional information
-
Clostridium sp.
Organism
Organism
UniProt
Commentary
Textmining
Clostridium kluyveri
-
-
-
Clostridium sp.
-
-
-
Reaction
Reaction
Commentary
Organism
Reaction ID
butanoate + NAD+ = but-2-enoate + NADH + H+
bi bi ping pong mechanism
Clostridium kluyveri
butanoate + NAD+ = but-2-enoate + NADH + H+
bi bi ping pong mechanism
Clostridium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(E)-2,5-dimethoxycinnamate + NADH
-
390679
Clostridium sp.
3-(2,5-dimethoxyphenyl)propionate + NAD+
-
-
-
?
(E)-2-butenoate + NADH
-
390679
Clostridium kluyveri
butanoate + NAD+
-
-
-
?
(E)-2-butenoate + NADH
-
390679
Clostridium sp.
butanoate + NAD+
-
-
-
?
(E)-2-methyl-2-butenoate + NADH
-
390679
Clostridium kluyveri
2-methylbutanoate + NAD+
-
-
-
?
(E)-2-methyl-2-butenoate + NADH
-
390679
Clostridium sp.
2-methylbutanoate + NAD+
-
-
-
?
(E)-4-methyl-2-pentenoate + NADH
-
390679
Clostridium kluyveri
4-methylpentanoate + NAD+
-
-
-
?
(E)-4-methyl-2-pentenoate + NADH
-
390679
Clostridium sp.
4-methylpentanoate + NAD+
-
-
-
?
(E)-cinnamate + NADH
-
390679
Clostridium kluyveri
phenylpropionate + NAD+
-
-
-
?
(E)-cinnamate + NADH
-
390679
Clostridium sp.
phenylpropionate + NAD+
-
-
-
?
(E)-o-hydroxycinnamate + NADH
-
390679
Clostridium kluyveri
3-(2-hydroxyphenyl)propionate + NAD+
-
-
-
?
(E)-o-hydroxycinnamate + NADH
-
390679
Clostridium sp.
3-(2-hydroxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-(dimethylamino)cinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-(dimethylamino)phenyl)propionate + NAD+
-
-
-
?
(E)-p-(dimethylamino)cinnamate + NADH
-
390679
Clostridium sp.
3-(4-(dimethylamino)phenyl)propionate + NAD+
-
-
-
?
(E)-p-chlorocinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(E)-p-chlorocinnamate + NADH
-
390679
Clostridium sp.
3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(E)-p-methoxycinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-methoxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-methoxycinnamate + NADH
-
390679
Clostridium sp.
3-(4-methoxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-nitrocinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-nitrophenyl)propionate + NAD+
-
-
-
?
(E)-p-nitrocinnamate + NADH
-
390679
Clostridium sp.
3-(4-nitrophenyl)propionate + NAD+
-
-
-
?
(E,E)-2,4-hexadienoate + NADH
-
390679
Clostridium sp.
? + NAD+
-
-
-
?
(R,S)-1-methyl-3-phenylallenecarboxylate + NADH
-
390679
Clostridium sp.
? + NAD+
-
-
-
?
(Z)-2-(formylamino)cinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-(formylamino)phenyl)propionate + NAD+
-
-
-
?
(Z)-2-(formylamino)cinnamate + NADH
-
390679
Clostridium sp.
3-(4-(formylamino)phenyl)propionate + NAD+
-
-
-
?
(Z)-2-chloro-3-(p-chlorophenyl)acrylate + NADH
-
390679
Clostridium sp.
2-chloro-3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(Z)-2-fluorocinnamate + NADH
-
390679
Clostridium sp.
3-(2-fluorophenyl)propionate + NAD+
-
-
-
?
(Z)-3-chlorocinnamate + NADH
-
390679
Clostridium sp.
3-(3-chlorophenyl)propionate + NAD+
-
-
-
?
butenoate + NADH
-
390679
Clostridium kluyveri
butanoate + NAD+
-
-
-
?
butenoate + NADH
-
390679
Clostridium sp.
butanoate + NAD+
-
-
-
?
monomethyl fumarate + NADH
-
390679
Clostridium sp.
4-methoxy-4-oxobutanoate + NAD+
-
-
-
?
additional information
transhydrogenase activity: reduction of 3-acetylpyridine adenine dinucleotide by NADH
390679
Clostridium kluyveri
?
-
-
-
?
additional information
transhydrogenase activity: reduction of 3-acetylpyridine adenine dinucleotide by NADH
390679
Clostridium sp.
?
-
-
-
?
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH-optima for transhydrogenase activity
Clostridium kluyveri
additional information
-
pH-optima for transhydrogenase activity
Clostridium sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
the enzyme splits off exclusively the (4S)-hydrogen
Clostridium kluyveri
NADH
the enzyme splits off exclusively the (4S)-hydrogen
Clostridium sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
the enzyme splits off exclusively the (4S)-hydrogen
Clostridium kluyveri
NADH
the enzyme splits off exclusively the (4S)-hydrogen
Clostridium sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
3-Phenylpropionate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
3-Phenylpropionate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
4-phenylbutanoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
4-phenylbutanoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
benzoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
benzoate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
dicoumarol
blocks the NAD-binding domain
Clostridium kluyveri
dicoumarol
blocks the NAD-binding domain
Clostridium sp.
fumarate
-
Clostridium kluyveri
fumarate
-
Clostridium sp.
morin
blocks the NAD-binding domain
Clostridium kluyveri
morin
blocks the NAD-binding domain
Clostridium sp.
NAD+
mixed-type inhibitor
Clostridium kluyveri
NAD+
mixed-type inhibitor
Clostridium sp.
phenylacetate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium kluyveri
phenylacetate
inhibits reduction of (E)-2-methyl-2-butenoate
Clostridium sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
-
Clostridium kluyveri
additional information
-
additional information
-
Clostridium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(E)-2,5-dimethoxycinnamate + NADH
-
390679
Clostridium sp.
3-(2,5-dimethoxyphenyl)propionate + NAD+
-
-
-
?
(E)-2-butenoate + NADH
-
390679
Clostridium kluyveri
butanoate + NAD+
-
-
-
?
(E)-2-butenoate + NADH
-
390679
Clostridium sp.
butanoate + NAD+
-
-
-
?
(E)-2-methyl-2-butenoate + NADH
-
390679
Clostridium kluyveri
2-methylbutanoate + NAD+
-
-
-
?
(E)-2-methyl-2-butenoate + NADH
-
390679
Clostridium sp.
2-methylbutanoate + NAD+
-
-
-
?
(E)-4-methyl-2-pentenoate + NADH
-
390679
Clostridium kluyveri
4-methylpentanoate + NAD+
-
-
-
?
(E)-4-methyl-2-pentenoate + NADH
-
390679
Clostridium sp.
4-methylpentanoate + NAD+
-
-
-
?
(E)-cinnamate + NADH
-
390679
Clostridium kluyveri
phenylpropionate + NAD+
-
-
-
?
(E)-cinnamate + NADH
-
390679
Clostridium sp.
phenylpropionate + NAD+
-
-
-
?
(E)-o-hydroxycinnamate + NADH
-
390679
Clostridium kluyveri
3-(2-hydroxyphenyl)propionate + NAD+
-
-
-
?
(E)-o-hydroxycinnamate + NADH
-
390679
Clostridium sp.
3-(2-hydroxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-(dimethylamino)cinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-(dimethylamino)phenyl)propionate + NAD+
-
-
-
?
(E)-p-(dimethylamino)cinnamate + NADH
-
390679
Clostridium sp.
3-(4-(dimethylamino)phenyl)propionate + NAD+
-
-
-
?
(E)-p-chlorocinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(E)-p-chlorocinnamate + NADH
-
390679
Clostridium sp.
3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(E)-p-methoxycinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-methoxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-methoxycinnamate + NADH
-
390679
Clostridium sp.
3-(4-methoxyphenyl)propionate + NAD+
-
-
-
?
(E)-p-nitrocinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-nitrophenyl)propionate + NAD+
-
-
-
?
(E)-p-nitrocinnamate + NADH
-
390679
Clostridium sp.
3-(4-nitrophenyl)propionate + NAD+
-
-
-
?
(E,E)-2,4-hexadienoate + NADH
-
390679
Clostridium sp.
? + NAD+
-
-
-
?
(R,S)-1-methyl-3-phenylallenecarboxylate + NADH
-
390679
Clostridium sp.
? + NAD+
-
-
-
?
(Z)-2-(formylamino)cinnamate + NADH
-
390679
Clostridium kluyveri
3-(4-(formylamino)phenyl)propionate + NAD+
-
-
-
?
(Z)-2-(formylamino)cinnamate + NADH
-
390679
Clostridium sp.
3-(4-(formylamino)phenyl)propionate + NAD+
-
-
-
?
(Z)-2-chloro-3-(p-chlorophenyl)acrylate + NADH
-
390679
Clostridium sp.
2-chloro-3-(4-chlorophenyl)propionate + NAD+
-
-
-
?
(Z)-2-fluorocinnamate + NADH
-
390679
Clostridium sp.
3-(2-fluorophenyl)propionate + NAD+
-
-
-
?
(Z)-3-chlorocinnamate + NADH
-
390679
Clostridium sp.
3-(3-chlorophenyl)propionate + NAD+
-
-
-
?
butenoate + NADH
-
390679
Clostridium kluyveri
butanoate + NAD+
-
-
-
?
butenoate + NADH
-
390679
Clostridium sp.
butanoate + NAD+
-
-
-
?
monomethyl fumarate + NADH
-
390679
Clostridium sp.
4-methoxy-4-oxobutanoate + NAD+
-
-
-
?
additional information
transhydrogenase activity: reduction of 3-acetylpyridine adenine dinucleotide by NADH
390679
Clostridium kluyveri
?
-
-
-
?
additional information
transhydrogenase activity: reduction of 3-acetylpyridine adenine dinucleotide by NADH
390679
Clostridium sp.
?
-
-
-
?
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
additional information
-
pH-optima for transhydrogenase activity
Clostridium kluyveri
additional information
-
pH-optima for transhydrogenase activity
Clostridium 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)
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
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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740951
Sun
Aerobic biosynthesis of hydroc ...
Clostridium acetobutylicum
Metab. Eng.
35
75-82
2016
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-
1
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4
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2
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1
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1
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2
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728964
Gall
Enzymatic conversion of flavon ...
Eubacterium ramulus
Angew. Chem. Int. Ed. Engl.
53
1439-1442
2014
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1
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1
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4
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2
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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
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-
1
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-
-
3
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2
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9
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1
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4
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2
2
3
1
3
1
2
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3
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1
3
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3
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2
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1
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4
-
2
3
1
3
1
2
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3
3
724734
Romagnolo
-
Fungal laccases and enoate red ...
Absidia glauca, Penicillium citrinum
Chem. Eng. Technol.
32
961-966
2013
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739971
Skrobiszewski
-
Pleurotus ostreatus as a sourc ...
Pleurotus ostreatus, Pleurotus ostreatus PO310783
Biocatal. Agricult. Biotechnol.
2
26-31
2013
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2
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12
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1
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1
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1
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12
-
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740318
Classen
-
Revisiting the enantioselectiv ...
Solanum lycopersicum, Photorhabdus luminescens
ChemCatChem
5
711-713
2013
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1
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2
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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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10
2
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741094
Paul
Mimicking nature: Synthetic ni ...
Thermus scotoductus
Org. Lett.
15
180-183
2013
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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
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724073
Liu
Asymmetric bioreduction of act ...
Achromobacter sp.
Appl. Microbiol. Biotechnol.
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Asymmetric reduction of activa ...
Gluconobacter oxydans
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39
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3
1
1
1
1
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686271
Stuermer
Asymmetric bioreduction of act ...
Saccharomyces cerevisiae, Burkholderia sp., Marchantia polymorpha, Rhodotorula sp., Rhodotorula
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Bacillus subtilis, Solanum lycopersicum
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12
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657039
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Biosynthesis of costunolide, d ...
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3
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Enoate reductases of Clostridi ...
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2
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1
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4
1
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1
1
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EPR and Moessbauer spectroscop ...
Clostridium tyrobutyricum
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1
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Clostridium sp.
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2
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-
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390669
Preiss
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Additional enoates amd other a ...
Clostridium tyrobutyricum
DECHEMA Biotechnol. Conf.
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1989
-
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8
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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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-
-
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-
-
-
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-
390670
Krause
Design and application of sens ...
Clostridium sporogenes, Moorella thermoacetica, Clostridium tyrobutyricum
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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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3
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3
-
3
-
-
-
-
-
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-
-
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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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2
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1
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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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-
-
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390674
Thanos
-
Electro-enzymic viologen-media ...
Clostridium tyrobutyricum
J. Biotechnol.
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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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-
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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
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390676
Bader
-
ATP formation is coupled to th ...
Clostridium sporogenes
FEMS Microbiol. Lett.
20
171-175
1983
-
-
-
-
-
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1
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-
-
2
-
-
-
-
-
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-
-
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-
-
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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
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1983
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33
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11
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11
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33
-
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-
-
-
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-
-
-
-
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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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4
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4
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4
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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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-
-
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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
-
2
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-
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31
-
-
-
-
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2
-
-
-
-
-
-
-
-
-
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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1
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-
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3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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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-
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2
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2
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-
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6
-
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-
-
-
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-
-
-
-
-
-
-
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390682
Bader
The activities of hydrogenase ...
Clostridium kluyveri, Clostridium sp.
Arch. Microbiol.
127
279-287
1980
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2
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5
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4
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2
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2
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2
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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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-
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4
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10
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4
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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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-
-
-
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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
-
1
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-
3
-
-
-
-
-
-
3
-
-
-
-
3
-
5
-
1
2
-
-
-
-
1
-
-
1
1
13
1
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1
-
1
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-
-
-
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-