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Information on EC 1.3.1.44 - trans-2-enoyl-CoA reductase (NAD+)
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EC Tree
1.3.1.44 trans-2-enoyl-CoA reductase (NAD+)IUBMB Comments
The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
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Word Map
- 1.3.1.44
- clostridium
-
biofuels
- acetobutylicum
-
treponema
- denticola
- 1-butanol
- butyryl-coa
- crotonase
- euglena
- gracilis
- enoyl-coas
- acyl-coas
-
thiolase
- propionyl-coa
- ferredoxins
-
coa-dependent
-
longer-chain
-
enoyl-acyl
-
feedstock
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
trans-enoyl-coa reductase, tdter, trans-2-enoyl-coa reductases, trans-2-enoyl-acp reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BatG
Tde_0597
tdTer
TER
trans-2-enoyl-ACP reductase
trans-2-enoyl-CoA reductase
trans-2-enoyl-CoA reductases
trans-enoyl-CoA reductase
additional information
additional information
-
enzyme belongs to the short-chain dehydrogenase/reductase family, enzyme is a component of fatty acid synthase type II
additional information
-
BatG as a trans-2-enoyl-ACP reductase isozyme, an isozyme of FabI, it contains the conserved NADH-binding motif GxxxGxG and catalytic triad YYK
additional information
-
BatG as a trans-2-enoyl-ACP reductase isozyme, an isozyme of FabI, it contains the conserved NADH-binding motif GxxxGxG and catalytic triad YYK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+
-
-
-
-
acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+
short chain-length specific
-
acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+
the enzyme of Euglena gracilis acts on crotonyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:NAD+ trans-2-oxidoreductase
The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA.
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CAS REGISTRY NUMBER
COMMENTARY
77649-64-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-didehydroacyl-CoA + NAD(P)H
acyl-CoA + NAD(P)+
i.e. enoyl-CoA
-
-
?
(E)-2-hexanoyl-CoA + NADPH
hexanoyl-CoA + NADP+
-
-
-
?
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
-
contributes to fatty acid synthesis beta-oxidation in mitochondria
-
-
?
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
-
fatty acid elongation
-
-
?
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
high activity toward crotonyl-CoA
-
-
?
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
-
high activity toward crotonyl-CoA
-
-
?
crotonyl-CoA + NADH
butyryl-CoA + NAD+
-
negative cooperativity in the reaction with substrate
-
-
?
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
-
crotonyl-CoA is reduced to butyryl-CoA by NADH, but not by NADPH, only in the presence of flavin nucleotides (FMN or FAD)
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
NADPH is a poor cosubstrate
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
NADPH is a poor cosubstrate
-
-
?
hexenoyl-CoA + NADH
? + NAD+
weak activity toward crotonyl-CoA
-
-
?
hexenoyl-CoA + NADH
? + NAD+
-
weak activity toward crotonyl-CoA
-
-
?
trans-2-decenoyl-CoA + NADH
decanoyl-CoA + NAD+
-
reductase II: highest activity
-
-
?
trans-2-dodecenoyl-CoA + NADH
dodecanoyl-CoA + NAD+
-
-
i.e. laurate
?
trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
-
-
-
?
trans-2-hexadecenoyl-CoA + NADH
hexadecanoyl-CoA + NAD+
-
-
-
-
?
trans-2-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NAD(P)+
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reductase III: highest activity, utilizes substrates of chain length C4-C12
-
-
?
trans-2-octenoyl-CoA + NADH
octanoyl-CoA + NAD+
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reductase II: highest activity
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-
?
additional information
?
-
no activity with butanoyl-CoA
-
-
?
additional information
?
-
-
reductase isoforms are chain length-specific
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-
?
additional information
?
-
enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
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-
?
additional information
?
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enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
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-
?
additional information
?
-
-
inert to substrates with chain length below C8
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-
?
additional information
?
-
-
inert to substrates with chain length below C8
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-
?
additional information
?
-
-
rat hepatic microsomal long-chain and short-chain trans-2-enoyl-CoA reductases with cofactor requirement (NADH or NADPH) depending on substrate chain length are characterized. Since no cis-2-enoyl-CoA compounds are tested as substrates a classification according to EC 1.3.1.8, EC 1.3.1.38 or EC 1.3.1.44 is impossible
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
trans-didehydroacyl-CoA + NAD(P)H
acyl-CoA + NAD(P)+
i.e. enoyl-CoA
-
-
?
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
-
contributes to fatty acid synthesis beta-oxidation in mitochondria
-
-
?
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
-
fatty acid elongation
-
-
?
additional information
?
-
enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
-
-
?
additional information
?
-
-
enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
about two-to threefold higher specific activites with NADH over NADPH
NADPH
-
enzyme utilizes NADH and NADPH depending on chain length, with NADPH a C-6 substrate is preferred, with NADH a C-8 substrate is preferred
NADPH
-
rat hepatic microsomal trans-2-enoyl-CoA reductases with cofactor requirement (NADH or NADPH) depending on chain length of substrates are characterized. Since no cis-2-enoyl-CoA substances are tested as substrates a classification according to EC 1.3.1.8, EC 1.3.1.38 or EC 1.3.1.44 is impossible
NADPH
about two-to threefold higher specific activites with NADH over NADPH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
substrates with chain-length higher than C16, concentration above 0.05 mM
-
additional information
-
substrates with chain-length higher than C16, concentrations above 0.02 mM
-
additional information
-
shows no inhibition by triclosan in a wide range of concentration (0.005-1 mM), or FAD (0.01 mM)
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
2-dodecenoyl-CoA
pH and temperature not specified in the publication, mutant I287A
0.109
Biochanin A
recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate
0.049
crotonyl-CoA
mutant Y240F, pH not specified in the publication, temperature not specified in the publication
0.049
crotonyl-CoA
pH and temperature not specified in the publication, mutant Y240F
0.06
crotonyl-CoA
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication
0.06
crotonyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A
0.068
crotonyl-CoA
recombinant enzyme, pH 6.2, 30°C, with NADH as cofactor
0.07
crotonyl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication
0.07
crotonyl-CoA
pH and temperature not specified in the publication, wild-type
0.1
crotonyl-CoA
mutant F295A, pH not specified in the publication, temperature not specified in the publication
0.1
crotonyl-CoA
pH and temperature not specified in the publication, mutant F295A
0.11
crotonyl-CoA
mutant L291A, pH not specified in the publication, temperature not specified in the publication
0.11
crotonyl-CoA
pH and temperature not specified in the publication, mutant L291A
0.15
crotonyl-CoA
mutant Y370A, pH not specified in the publication, temperature not specified in the publication
0.15
crotonyl-CoA
pH and temperature not specified in the publication, mutant Y370A
0.16
crotonyl-CoA
mutant I287A, pH not specified in the publication, temperature not specified in the publication
0.16
crotonyl-CoA
pH and temperature not specified in the publication, mutant I287A
0.21
crotonyl-CoA
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
0.21
crotonyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
0.0034
hexanoyl-CoA
pH and temperature not specified in the publication, mutant I287A
0.007
hexanoyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A
0.012
hexanoyl-CoA
pH and temperature not specified in the publication, wild-type
0.015
hexanoyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
0.018
hexanoyl-CoA
pH and temperature not specified in the publication, mutant Y370A
0.019
hexanoyl-CoA
pH and temperature not specified in the publication, mutant F295A
0.038
hexanoyl-CoA
pH and temperature not specified in the publication, mutant L291A
0.0052
NADH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.119
NADPH
recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate
0.19
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0011
trans-2-dodecenoyl-CoA
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
0.003
trans-2-dodecenoyl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication
0.004
trans-2-dodecenoyl-CoA
mutant I287A, pH not specified in the publication, temperature not specified in the publication
0.0034
trans-2-hexenoyl-CoA
mutant I287A, pH not specified in the publication, temperature not specified in the publication
0.007
trans-2-hexenoyl-CoA
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication
0.012
trans-2-hexenoyl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication
0.015
trans-2-hexenoyl-CoA
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
0.018
trans-2-hexenoyl-CoA
mutant Y370A, pH not specified in the publication, temperature not specified in the publication
0.019
trans-2-hexenoyl-CoA
mutant F295A, pH not specified in the publication, temperature not specified in the publication
0.038
trans-2-hexenoyl-CoA
mutant L291A, pH not specified in the publication, temperature not specified in the publication
0.091
trans-2-hexenoyl-CoA
recombinant enzyme, pH 6.2, 30°C, with NADH as cofactor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6
2-dodecenoyl-CoA
pH and temperature not specified in the publication, mutant I287A
24
2-dodecenoyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
90
2-dodecenoyl-CoA
pH and temperature not specified in the publication, wild-type
0.73
crotonyl-CoA
mutant Y240F, pH not specified in the publication, temperature not specified in the publication
0.73
crotonyl-CoA
pH and temperature not specified in the publication, mutant Y240F
7.1
crotonyl-CoA
mutant I287A, pH not specified in the publication, temperature not specified in the publication
7.1
crotonyl-CoA
pH and temperature not specified in the publication, mutant I287A
15.6
crotonyl-CoA
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication
15.6
crotonyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A
18.9
crotonyl-CoA
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
18.9
crotonyl-CoA
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
37
crotonyl-CoA
mutant L291A, pH not specified in the publication, temperature not specified in the publication
37
crotonyl-CoA
pH and temperature not specified in the publication, mutant L291A
73
crotonyl-CoA
mutant F295A, pH not specified in the publication, temperature not specified in the publication
73
crotonyl-CoA
pH and temperature not specified in the publication, mutant F295A
91
crotonyl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication