Information on EC 1.3.1.38 - trans-2-enoyl-CoA reductase (NADPH)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.3.1.38
-
RECOMMENDED NAME
GeneOntology No.
trans-2-enoyl-CoA reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
show the reaction diagram
stereospecificity of NADPH: pro-4S
-
acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
show the reaction diagram
mechanism: anti addition of hydrogen via a 2Re, 3Re attack on trans double bond
-
acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
show the reaction diagram
inducible by growth on oleic acid
-
acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH + H+
show the reaction diagram
inducible by growth on oleic acid, mechanism: anti addition of hydrogen via a 2Re, 3Re attack on trans double bond
Escherichia coli K12
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of unsaturated fatty acids
-
-
Fatty acid elongation
-
-
Metabolic pathways
-
-
phytol degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:NADP+ trans-2-oxidoreductase
Not identical with EC 1.3.1.37 cis-2-enoyl-CoA reductase (NADPH) [cf. EC 1.3.1.8 acyl-CoA dehydrogenase (NADP+)].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NADPH-dependent trans-2-enoyl-CoA reductase
-
-
-
-
reductase, trans-enoyl coenzyme A
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
77649-64-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
guinea pig
Uniprot
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
isoform ECR1
UniProt
Manually annotated by BRENDA team
isoform ECR2
UniProt
Manually annotated by BRENDA team
expression in Escherichia coli fused to maltose-binding protein
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
no information in the literature concerning reduction of cis-2-enoyl-CoA substrates, thus classification of rat enzyme according to EC 1.3.1.8 or EC 1.3.1.38 not yet possible
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
knockdown of MECR-1 resulted in life span extension
malfunction
-
functional analysis of PaECR1 is conducted by virus-induced gene silencing to knock down the gene expression in Phalaenopsis amabilis. The PaECR1-silenced plants are more susceptible to Erwinia chrysanthemi infection, implying potential roles for very long chain fatty acids in the pathogenesis
physiological function
-
up-regulated expression upon Erwinia chrysanthemi infection
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-dodecenoyl-acyl carrier protein + NADH
dodecanoyl-acyl carrier protein + NAD+
show the reaction diagram
-
-
-
-
?
2-dodecenoyl-CoA + NADH
dodecanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
2-trans-hexenoyl-CoA + NADPH
?
show the reaction diagram
O45903, Q9XXC8
-
-
-
?
acyl-CoA + NADP+
trans-2,3-dehydroacyl-CoA + NADPH
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
-
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
i.e. trans-2-butenoyl-CoA
-
?
nervonyl-CoA + NADPH
tetracosanoyl-CoA + NADP+
show the reaction diagram
-
-
1% of the activity with trans-phytenoyl-CoA
-
ir
octa-2-enoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
ir
trans-2,3-dehydrostearoyl-CoA + NADPH
stearoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2,3-dehydrostearoyl-CoA + NADPH
stearoyl-CoA + NADP+
show the reaction diagram
Q9CY27
-
-
-
?
trans-2-decenoyl-CoA + NADPH
decanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
-
trans-2-decenoyl-CoA + NADPH
decanoyl-CoA + NADP+
show the reaction diagram
Q9JIF5
highest activity with, native and recombinant enzyme
-
?
trans-2-decenoyl-CoA + NADPH
decanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
Q9JIF5
50% activity compared to that with trans-2-decenoyl-CoA, native and recombinant enzyme
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
trans-2-hexenoyl-CoA + NADPH + H+
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexenoyl-CoA + NADPH + H+
hexanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
Q9JIF5
50% activity compared to that with trans-2-decenoyl-CoA, native and recombinant enzyme
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
?
trans-2-octenoyl-CoA + NADPH
octanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
?
trans-2-octenoyl-CoA + NADPH + H+
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH + H+
octanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
?
trans-phytenoyl-CoA + NADPH + H+
phytanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
ir
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
additional information
?
-
-
no reduction of trans-2-tetradecenoyl-CoA
-
-
-
additional information
?
-
-
NADPH-specific trans-enoyl-CoA reductases from rat liver miochondria and microsomes impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates
-
-
-
additional information
?
-
-
activity decreases with increasing chain length of substrates
-
-
-
additional information
?
-
Q9JIF5
key enzyme in fatty acid chain elongation pathway
-
-
-
additional information
?
-
Escherichia coli K12
-
activity decreases with increasing chain length of substrates
-
-
-
additional information
?
-
Escherichia coli K12
-
no reduction of trans-2-tetradecenoyl-CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trans-2-hexenoyl-CoA + NADPH + H+
hexanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-hexenoyl-CoA + NADPH + H+
hexanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli K12
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH + H+
octanoyl-CoA + NADP+
show the reaction diagram
-
-
-
-
?
trans-2-octenoyl-CoA + NADPH + H+
octanoyl-CoA + NADP+
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
show the reaction diagram
-
i.e. trans-2-butenoyl-CoA
-
?
additional information
?
-
Q9JIF5
key enzyme in fatty acid chain elongation pathway
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
-
NADPH
-
specific for
NADPH
Q9JIF5
specific for
NADPH
A9XUG7, A9XUG8
the G(5X)IPXG motif represents a putative NADPH binding motif located in a loop between transmembrane domains 4 and 5; the G(5X)IPXG motif represents a putative NADPH binding motif located in a loop between transmembrane domains 4 and 5
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
i.e. DTNB, inhibition can be prevented by preincubation with NADPH, thus a SH-group is involved in cofactor binding
Bovine serum albumin
-
-
-
decanoyl-CoA
-
-
iodoacetic acid
-
-
myristoyl-CoA
-
-
N-ethylmaleimide
-
-
N-ethylmaleimide
Q9JIF5
native and recombinant enzyme
Octanoyl-CoA
-
-
p-hydroxymercuribenzoate
-
-
palmitoleoyl-CoA
-
-
palmitoyl-CoA
-
-
Saturated CoA analogs
-
-
-
Triton X-100
-
-
Lauroyl-CoA
-
-
additional information
-
not inhibitory: methylglyoxal
-
additional information
-
Zn2+, Fe3+, Mn2+, Mg2+, Ca2+, NH4+, Na+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no flavoprotein
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00433
2-dodecenoyl-CoA
-
mutant enzyme F149A, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
0.0054
2-dodecenoyl-CoA
-
wild type enzyme, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
0.0152
NADH
-
mutant enzyme F149A, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
0.0352
NADH
-
wild type enzyme, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
0.0049
NADPH
-
-
0.038
NADPH
Q9JIF5
-
0.053
NADPH
Q9JIF5
recombinant enzyme
0.106
NADPH
-
37C, pH 7.2
0.072
trans-2-crotonyl-CoA
-
-
0.0071
trans-2-decenoyl-CoA
-
-
0.011
trans-2-decenoyl-CoA
Q9JIF5
-
0.018
trans-2-decenoyl-CoA
Q9JIF5
recombinant enzyme
0.0037
trans-2-dodecenoyl-CoA
-
-
0.048
trans-2-Hexenoyl-CoA
-
-
0.011
trans-2-octenoyl-CoA
-
-
0.018
trans-phytenoyl-CoA
-
37C, pH 7.2
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
2-dodecenoyl-CoA
-
mutant enzyme F149A, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
3.17
2-dodecenoyl-CoA
-
wild type enzyme, at 25C in 30 mM PIPES and 150 mM NaCl (pH 6.8)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.063
decanoyl-CoA
-
-
0.045
Lauroyl-CoA
-
-
0.0092
myristoyl-CoA
-
-
0.198
Octanoyl-CoA
-
-
0.00054
palmitoleoyl-CoA
-
-
0.0025
palmitoyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.005
-
substrate crotonyl-CoA
0.05
-
substrate trans-hexenoyl-CoA
0.065
-
substrate trans-hexenoyl-CoA
0.0752
Q9JIF5
partially purified
0.2
O45903, Q9XXC8
mutant cells over-expressiong MECR-1; mutant cells over-expressiong MECR-1
0.346
Q9JIF5
purified recombinant enzyme
0.49
-
partially purified enzyme
3.21
O45903, Q9XXC8
cells overexpressing native Etr1p; cells overexpressing native Etr1p
20
-
purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
37
-
assay at
37
Q9JIF5
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
-
gel filtration
390748
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Q9JIF5
? * 32500-40000, sequence determination and SDS-PAGE
?
Q99MZ7
? * 32600, sequence determination
?
Q9BY49
? * 32300, sequence determination
?
-
x * 75000, calculated and SDs-PAGE of enzyme fused to maltose-binding protein
dimer
-
2 * 40000, SDS-PAGE
dimer
Escherichia coli K12
-
2 * 40000, SDS-PAGE
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 8
-
-
390749
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
15 min, pH 6.0-8.0
390749
56
-
10 min, pH 6.0, 50% inactivation but reactivation at pH 8.0
390749
60
-
10 min, inactivation
390749
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for at least a month, when stored at -20C in PBS containing 50% (v/v) glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, pH 7.0
-
-20C, Tris-HCl buffer, pH 8.0, 10% v/v glycerol
-
0C, pH 7.0, 1 mg per ml, 70% of activity remaining after 44 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
associated with peroxisomal acyldihydroxyacetone phosphate reductase; partial
Q9JIF5
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae DELTA etr1 cells; expression in Saccharomyces cerevisiae DELTA etr1 cells
O45903, Q9XXC8
expression as His-tagged protein in Escherichia coli, sequence analysis
Q9JIF5
-
Q9BY49
cloning of cDNA, expression of TER in HEK-293 cells
-
-
Q99MZ7
cloning of cDNA
Q9CY27
expressed in Escherichia coli BL21(DE3)pLysS cells
-
cloned and expressed in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is up-regulated during cotton fibre elongation
-
trans-2-enoyl-CoA reductase is one of the most abundant transcripts in the Erwinia chrysanthemi-induced EST library
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G225A
A9XUG7, A9XUG8
upon expression in Saccharomyces cerevisiae tsc13DELTA mutant significant accumulation of fatty acids C22:0, C20:0, C18:0, C18-OH, and especially C16-OH is detected
G227A
A9XUG7, A9XUG8
similar to wild-type
G228A
A9XUG7, A9XUG8
similar to wild-type
G234A
A9XUG7, A9XUG8
upon expression in Saccharomyces cerevisiae tsc13DELTA mutant significant accumulation of fatty acids C22:0, C20:0, C18:0, C18-OH, and especially C16-OH is detected
P232A
A9XUG7, A9XUG8
upon expression in Saccharomyces cerevisiae tsc13DELTA mutant significant accumulation of fatty acids C22:0, C20:0, C18:0, C18-OH, and especially C16-OH is detected
Q230A
A9XUG7, A9XUG8
similar to wild-type
R233A
A9XUG7, A9XUG8
similar to wild-type
S226A
A9XUG7, A9XUG8
similar to wild-type
Y229A
A9XUG7, A9XUG8
similar to wild-type
F149A
-
the mutant is not able to optimally position the cofactor for hydride transfer, which correlates with the 30fold decrease in kcat
K165A
-
normal expression in Escherichia coli
K165Q
-
normal expression in Escherichia coli
Y158F
-
expression in Escherichia coli sub-population BL21(DE3)NH
additional information
-
knockdown of MECR-1 resulted in life span extension
I231A
A9XUG7, A9XUG8
upon expression in Saccharomyces cerevisiae tsc13DELTA mutant significant accumulation of fatty acids C22:0, C20:0, C18:0, C18-OH, and especially C16-OH is detected
additional information
-
enzyme is able to rescue the growth of the Saccharomyces cerevisiae tsc13DELTA mutant