BRENDA - Enzyme Database
show all sequences of 1.3.1.34

Studies of human 2,4-dienoyl CoA reductase shed new light on peroxisomal betta-oxidation of unsaturated fatty acids

Hua, T.; Wu, D.; Ding, W.; Wang, J.; Shaw, N.; Liu, Z.J.; J. Biol. Chem. 287, 28956-28965 (2012)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escehrichia coli as a His-tagged fusion protein
Homo sapiens
Crystallization (Commentary)
Crystallization (Commentary)
Organism
the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate
Homo sapiens
Engineering
Protein Variants
Commentary
Organism
D137A
relative activity: 3.32% (substrate: 2,4-decadienoyl CoA), 1.27% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D155A
relative activity: 36.3% (substrate: 2,4-decadienoyl CoA), 59.6% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D186A
relative activity: 6.21% (substrate: 2,4-decadienoyl CoA), 1.86% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D268A
relative activity: 2.75% (substrate: 2,4-decadienoyl CoA), 1.14% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D86A
relative activity: 1.70% (substrate: 2,4-decadienoyl CoA), 1.76% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
E215A
relative activity: 28.9% (substrate: 2,4-decadienoyl CoA), 7.59% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0127
-
(2E,4E)-2,4-decadienoyl-CoA
pH 7.4, 20°C
Homo sapiens
0.0716
-
(2E,4E)-2,4-hexadienoyl-CoA
pH 7.4, 20°C
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
peroxisome
-
Homo sapiens
5777
-
Organism
Organism
UniProt
Commentary
Textmining
Homo sapiens
Q9NUI1
-
-
Purification (Commentary)
Purification (Commentary)
Organism
Ni-NTA chromatography
Homo sapiens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(2E,4E)-2,4-decadienoyl-CoA + NADPH
-
725482
Homo sapiens
?
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH
-
725482
Homo sapiens
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
More
analytical ultracentrifugation analysis of purified pDCR reveals that the protein exists as a mixture of monomers, dimers, and tetramers in solution
Homo sapiens
Synonyms
Synonyms
Commentary
Organism
pDCR
-
Homo sapiens
peroxisomal 2,4-dienoyl CoA reductase
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escehrichia coli as a His-tagged fusion protein
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
the crystal structure of a ternary complex of peroxisomal 2,4-dienoyl CoA reductases (pDCR) with hexadienoyl CoA and NADP is described. The structure of pDCR refined to 1.84 A resolution reveals the absence of the tyrosine-serine pair seen in the active site of mitochondrial DCR. Instead, aspartate hydrogen-bonded to the Calpha hydroxyl via a water molecule perturbs the water molecule for protonation of the substrate
Homo sapiens
Engineering (protein specific)
Protein Variants
Commentary
Organism
D137A
relative activity: 3.32% (substrate: 2,4-decadienoyl CoA), 1.27% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D155A
relative activity: 36.3% (substrate: 2,4-decadienoyl CoA), 59.6% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D186A
relative activity: 6.21% (substrate: 2,4-decadienoyl CoA), 1.86% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D268A
relative activity: 2.75% (substrate: 2,4-decadienoyl CoA), 1.14% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
D86A
relative activity: 1.70% (substrate: 2,4-decadienoyl CoA), 1.76% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
E215A
relative activity: 28.9% (substrate: 2,4-decadienoyl CoA), 7.59% (substrate: 2,4-hexadienoyl CoA) (wild-type: 100%)
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0127
-
(2E,4E)-2,4-decadienoyl-CoA
pH 7.4, 20°C
Homo sapiens
0.0716
-
(2E,4E)-2,4-hexadienoyl-CoA
pH 7.4, 20°C
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
peroxisome
-
Homo sapiens
5777
-
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA chromatography
Homo sapiens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(2E,4E)-2,4-decadienoyl-CoA + NADPH
-
725482
Homo sapiens
?
-
-
-
?
(2E,4E)-2,4-hexadienoyl-CoA + NADPH
-
725482
Homo sapiens
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
More
analytical ultracentrifugation analysis of purified pDCR reveals that the protein exists as a mixture of monomers, dimers, and tetramers in solution
Homo sapiens
Other publictions for EC 1.3.1.34
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)
725482
Hua
Studies of human 2,4-dienoyl C ...
Homo sapiens
J. Biol. Chem.
287
28956-28965
2012
-
-
1
1
6
-
-
2
1
-
-
-
-
1
-
-
1
-
-
-
-
-
2
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
6
-
-
-
-
2
1
-
-
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
685196
Tu
Two distinct proton donors at ...
Escherichia coli
Biochemistry
47
1167-1175
2008
-
-
1
-
8
-
-
6
-
1
-
-
-
6
-
-
1
-
-
-
7
-
2
-
1
-
-
-
6
-
-
-
2
-
-
-
-
-
1
2
-
8
-
-
-
-
6
-
1
-
-
-
-
-
1
-
-
7
-
2
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
652365
Ren
Metabolic functions of the two ...
Rattus norvegicus
J. Biol. Chem.
278
111-116
2003
-
-
-
-
-
-
1
1
1
-
-
2
-
2
-
-
1
-
-
1
-
-
4
-
1
-
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
1
1
-
-
2
-
-
-
1
-
1
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
656161
Hubbard
The crystal structure and reac ...
Escherichia coli
J. Biol. Chem.
278
37553-37560
2003
-
-
1
1
-
-
-
-
-
1
-
-
-
9
-
-
1
1
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
657265
Chu
Expression, purification, and ...
Homo sapiens
Protein Expr. Purif.
31
292-297
2003
-
-
1
-
-
-
-
3
3
-
1
1
-
8
-
-
1
-
-
-
1
3
3
1
2
1
-
1
-
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
3
3
-
1
1
-
-
-
1
-
-
1
3
3
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
390725
De Nys
Characterisation of human pero ...
Homo sapiens
Biochim. Biophys. Acta
1533
66-72
2001
-
-
1
-
-
-
1
3
4
-
1
-
-
7
-
-
-
-
-
1
-
1
4
-
1
1
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
1
-
3
4
-
1
-
-
-
-
-
-
1
-
1
4
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
390724
Liang
2,4-Dienoyl-CoA reductase from ...
Escherichia coli
Arch. Biochem. Biophys.
380
373-379
2000
-
-
1
-
-
-
-
-
-
1
-
-
-
6
-
-
-
-
-
-
-
-
4
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
1
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390720
Gruvitz
The Saccharomyces cerevisiae p ...
Saccharomyces cerevisiae
J. Biol. Chem.
272
22140-22147
1997
-
-
1
-
-
-
-
-
2
-
2
-
-
11
-
-
1
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
1
-
-
1
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390721
He
Cloning and expression of the ...
Escherichia coli
Eur. J. Biochem.
248
516-520
1997
-
-
1
-
-
-
-
2
-
-
1
-
-
6
-
-
-
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
390708
Mizugaki
Studies on the metabolism of u ...
Escherichia coli, Escherichia coli B / ATCC 11303
J. Biochem.
91
1453-1456
1982
-
-
-
-
-
-
2
-
-
-
-
-
-
182
-
-
1
-
-
-
-
-
2
-
1
-
-
-
-
1
-
3
1
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
390710
Dommes
Purification by affinity chrom ...
Bos taurus, Escherichia coli
Eur. J. Biochem.
125
335-341
1982
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
2
-
-
2
2
-
2
-
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
2
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-