BRENDA - Enzyme Database show
show all sequences of 1.3.1.86

Crotonyl coenzyme A reductase activity of bovine mammary fatty acid synthetase

Maitra, S.K.; Kumar, S.; J. Biol. Chem. 249, 111-117 (1974)

Data extracted from this reference:

General Stability
General Stability
Organism
the crotonyl-CoA reductase activity is influenced by preincubation. 0.25 M Tris-HCl buffer diminishes the crotonyl-CoA reductase activity by approximately 30%
Bos taurus
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
at high concentrations beta-mercaptoethanol is inhibitory
Bos taurus
dithiothreitol
at high concentrations dithiothreitol is inhibitory
Bos taurus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0033
-
trans-crotonyl-CoA
in 200 mM potassium phosphate buffer, pH 6.8, at 26C
Bos taurus
0.00364
-
NADPH
in 200 mM potassium phosphate buffer, pH 6.8, at 26C
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Purification (Commentary)
Commentary
Organism
ammonium sulfate precipitation, calcium phosphate gel treatment, alumina gel Cgamma extract filtration, Sephadex G-200 gel filtration
Bos taurus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
mammary gland
-
Bos taurus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.0061
-
crude extract, pH 6.8, at 26C
Bos taurus
0.0501
-
after 11.2fold purification, pH 6.8, at 26C
Bos taurus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
390852
Bos taurus
?
-
-
-
-
trans-crotonyl-CoA + NADPH + H+
the crotonyl-CoA reductase reaction requires NADPH as electron donor
390852
Bos taurus
butyryl-CoA + NADP+
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Bos taurus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8.5
-
Bos taurus
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
Bos taurus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
Bos taurus
General Stability (protein specific)
General Stability
Organism
the crotonyl-CoA reductase activity is influenced by preincubation. 0.25 M Tris-HCl buffer diminishes the crotonyl-CoA reductase activity by approximately 30%
Bos taurus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-mercaptoethanol
at high concentrations beta-mercaptoethanol is inhibitory
Bos taurus
dithiothreitol
at high concentrations dithiothreitol is inhibitory
Bos taurus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0033
-
trans-crotonyl-CoA
in 200 mM potassium phosphate buffer, pH 6.8, at 26C
Bos taurus
0.00364
-
NADPH
in 200 mM potassium phosphate buffer, pH 6.8, at 26C
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
ammonium sulfate precipitation, calcium phosphate gel treatment, alumina gel Cgamma extract filtration, Sephadex G-200 gel filtration
Bos taurus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
mammary gland
-
Bos taurus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.0061
-
crude extract, pH 6.8, at 26C
Bos taurus
0.0501
-
after 11.2fold purification, pH 6.8, at 26C
Bos taurus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
390852
Bos taurus
?
-
-
-
-
trans-crotonyl-CoA + NADPH + H+
the crotonyl-CoA reductase reaction requires NADPH as electron donor
390852
Bos taurus
butyryl-CoA + NADP+
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
37
-
-
Bos taurus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
8.5
-
Bos taurus
Other publictions for EC 1.3.1.86
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)
725287
Aboulnaga
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3704-3713
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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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1
1
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4
4
712235
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Biosynthesis of salinosporamid ...
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J. Am. Chem. Soc.
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10376-10377
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712641
Akopiants
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Streptomyces cinnamonensis
J. Ind. Microbiol. Biotechnol.
33
141-150
2006
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1
1
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656737
Li
Crotonyl-coenzyme A reductase ...
Streptomyces cinnamonensis, Streptomyces collinus
Microbiology
150
3463-3472
2004
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1
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2
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4
4
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711366
Fukui
Engineering of Ralstonia eutro ...
Streptomyces cinnamonensis
Biomacromolecules
3
618-624
2002
1
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1
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4
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1
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1
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1
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1
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712939
Liu
Precursor supply for polyketid ...
Streptomyces cinnamonensis
Metab. Eng.
3
40-48
2001
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3
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1
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1
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1
1
1
1
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-
712617
Sun
-
Crotonic acid-directed biosynt ...
Streptomyces hygroscopicus subsp. ascomyceticus
J. Ferment. Bioeng.
86
261-265
1998
-
-
-
-
-
-
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-
-
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1
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1
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1
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1
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713435
Stassi
Ethyl-substituted erythromycin ...
Streptomyces collinus
Proc. Natl. Acad. Sci. USA
95
7305-7309
1998
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1
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3
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2
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2
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1
1
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712233
Liu
-
Linking diversity in evolution ...
Streptomyces collinus
J. Am. Chem. Soc.
119
2973-2979
1997
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1
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1
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712270
Han
A novel alternate anaplerotic ...
Streptomyces collinus
J. Bacteriol.
179
5157-5164
1997
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5
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1
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2
2
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711884
Wallace
Purification of crotonyl-CoA r ...
Streptomyces collinus
Eur. J. Biochem.
233
954-962
1995
1
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1
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19
2
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3
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3
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1
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4
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2
1
1
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1
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1
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1
6
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1
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1
1
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19
6
2
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3
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1
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4
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2
1
1
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1
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1
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1
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711170
Dodds
-
Effects of coenzyme A and pH o ...
Bos taurus
Biochem. Soc. Trans.
9
556-557
1981
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390850
Strom
-
Activation and inhibition of c ...
Bos taurus
J. Biol. Chem.
254
8159-8162
1979
1
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9
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1
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4
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1
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390852
Maitra
Crotonyl coenzyme A reductase ...
Bos taurus
J. Biol. Chem.
249
111-117
1974
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1
2
2
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1
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