BRENDA - Enzyme Database
show all sequences of 1.3.1.44

Enzymology of butyrate formation by Butyrivibrio fibrisolvens

Miller, T.L.; Jenesel, S.E.; J. Bacteriol. 138, 99-104 (1979)

Data extracted from this reference:

Organism
Organism
UniProt
Commentary
Textmining
Butyrivibrio fibrisolvens
-
strain D1
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.79
-
in 100 mM PIPES (pH 7.0), at 22°C
Butyrivibrio fibrisolvens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
crotonyl-CoA + NADH + H+
crotonyl-CoA is reduced to butyryl-CoA by NADH, but not by NADPH, only in the presence of flavin nucleotides (FMN or FAD)
286051
Butyrivibrio fibrisolvens
butyryl-CoA + NAD+
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
crotonyl-CoA reductase, NAD-linked
-
Butyrivibrio fibrisolvens
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Butyrivibrio fibrisolvens
FMN
-
Butyrivibrio fibrisolvens
NADH
-
Butyrivibrio fibrisolvens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Butyrivibrio fibrisolvens
FMN
-
Butyrivibrio fibrisolvens
NADH
-
Butyrivibrio fibrisolvens
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.79
-
in 100 mM PIPES (pH 7.0), at 22°C
Butyrivibrio fibrisolvens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
crotonyl-CoA + NADH + H+
crotonyl-CoA is reduced to butyryl-CoA by NADH, but not by NADPH, only in the presence of flavin nucleotides (FMN or FAD)
286051
Butyrivibrio fibrisolvens
butyryl-CoA + NAD+
-
-
-
?
Other publictions for EC 1.3.1.44
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)
740212
Schadeweg
Increasing n-butanol productio ...
Treponema denticola, Treponema denticola VSY0
Biotechnol. Biofuels
9
257
2016
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724240
Hu
Structures of trans-2-enoyl-Co ...
Treponema denticola, Clostridium acetobutylicum, Treponema denticola ATCC 35405
Biochem. J.
449
79-89
2013
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2
4
10
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10
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3
2
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17
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2
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10
4
8
2
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10
2
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4
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2
4
4
10
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10
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3
2
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2
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10
4
2
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10
2
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10
10
724351
Bond-Watts
Biochemical and structural cha ...
Treponema denticola, Treponema denticola ATCC 35405
Biochemistry
51
6827-6837
2012
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1
2
7
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3
36
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5
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11
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36
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14
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1
2
2
7
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3
14
36
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11
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36
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38
38
723850
Lee
Crystallization and preliminar ...
Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
67
214-216
2011
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1
1
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1
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711734
Mattheus
The kalimantacin/batumin biosy ...
Pseudomonas fluorescens, Pseudomonas fluorescens BCCM_ID9359
Chem. Biol.
17
1067-1071
2010
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1
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1
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4
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2
2
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686722
Tucci
A novel prokaryotic trans-2-en ...
Treponema denticola
FEBS Lett.
581
1561-1566
2007
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1
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1
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1
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1
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1
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2
1
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656287
Hoffmeister
Mitochondrial trans-2-enoyl-Co ...
Euglena gracilis
J. Biol. Chem.
280
4329-4338
2005
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1
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8
1
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1
2
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16
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2
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1
8
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5
2
2
1
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1
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4
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1
4
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8
1
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1
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2
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1
8
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5
2
1
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1
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657270
Poletto
Selection of an Escherichia co ...
Mycobacterium tuberculosis
Protein Expr. Purif.
34
118-125
2004
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1
1
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4
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1
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1
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390806
Inui
Purification and some properti ...
Euglena gracilis
J. Biochem.
100
995-1000
1986
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7
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1
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3
1
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1
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1
1
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1
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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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2
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7
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1
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3
1
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1
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1
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2
1
1
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1
1
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390810
Inui
Fatty acid synthesis in mitoch ...
Euglena gracilis
Eur. J. Biochem.
142
121-126
1984
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1
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1
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5
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390754
Nagi
Biochemical properties of shor ...
Rattus norvegicus
Arch. Biochem. Biophys.
226
50-64
1983
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2
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390755
Prasad
Kinetic evidence for two separ ...
Rattus norvegicus
Biochem. Biophys. Res. Commun.
113
659-665
1983
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1
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3
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3
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1
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390807
Shimakata
Purification and characterizat ...
Mycolicibacterium smegmatis
J. Biochem.
89
1075-1080
1981
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-
-
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4
5
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1
1
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1
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1
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1
1
9
1
1
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1
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1
1
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1
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4
1
5
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1
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1
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1
1
9
1
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1
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390808
Shimakata
Involvement of one of two enoy ...
Mycolicibacterium smegmatis
J. Biochem.
88
1051-1058
1980
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1
1
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1
1
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1
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1
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1
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5
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1
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1
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1
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1
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1
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5
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1
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286051
Miller
Enzymology of butyrate formati ...
Butyrivibrio fibrisolvens
J. Bacteriol.
138
99-104
1979
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1
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1
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1
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