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Information on EC 1.3.1.44 - trans-2-enoyl-CoA reductase (NAD+)
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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
-
biofuels
- 1-butanol
- butyryl-coa
- acetobutylicum
-
treponema
- denticola
- propionyl-coa
-
enoyl-acyl
- ferredoxins
- gracilis
-
longer-chain
- enoyl-coas
-
coa-dependent
-
feedstock
-
clostridial
- crotonase
- acyl-coas
- euglena
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
2-enoyl-reductase, BatG, CaTER, crotonyl-CoA reductase, NAD-linked, enoyl-acyl carrier protein reductase, ENR, FabI, More, Tde_0597, tdTer, 
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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+
; the enzyme of Euglena gracilis acts on crotonyl-CoA and, more slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA
-
-
-
acyl-CoA + NAD+ = trans-didehydroacyl-CoA + NADH + H+
short chain-length specific
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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
-
-
-
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)+
-
reductase III: highest activity, utilizes substrates of chain length C4-C12
-
-
-
trans-2-octenoyl-CoA + NADH
octanoyl-CoA + NAD+
-
reductase II: highest activity
-
-
?
additional information
?
-
no activity with butanoyl-CoA
-
-
-
additional information
?
-
-
reductase isoforms are chain length-specific
-
-
-
additional information
?
-
enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
-
-
-
additional information
?
-
-
inert to substrates with chain length below C8
-
-
-
additional information
?
-
-
inert to substrates with chain length below C8
-
-
-
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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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)+
Q5EU90
i.e. enoyl-CoA
-
-
?
additional information
?
-
Q5EU90
enzyme is involved in malonyl-CoA independent lipid synthesis and wax ester fermentation
-
-
-
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
-
-
-
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
-
fatty acid elongation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
about two-to threefold higher specific activites with NADH over NADPH; preferred, 2-3fold higher activity compared to NADPH
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
-
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
2-3fold lower activity compared to the preferred NADH; 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
0.049
crotonyl-CoA
-
mutant Y240F, pH not specified in the publication, temperature not specified in the publication; 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; pH and temperature not specified in the publication, mutant L276A/V277A
0.068
crotonyl-CoA
pH 6.2, 30°C; recombinant enzyme, pH 6.2, 30°C, with NADH as cofactor
0.07
crotonyl-CoA
-
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
0.1
crotonyl-CoA
-
mutant F295A, pH not specified in the publication, temperature not specified in the publication; 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; 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; 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; 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; 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
0.0316
NADH
mutant enzyme F11K, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant F11K
0.1054
NADH
pH 6.2, 25°C; wild type enzyme, at pH 6.2 and 25°C
0.109
NADH
cosubstrate crotonyl-CoA, pH 6.2, 30°C; recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate
0.119
NADPH
cosubstrate crotonyl-CoA, pH 6.2, 30°C; 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
pH 6.2, 30°C; 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; 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; 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; 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; 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; 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; pH and temperature not specified in the publication, mutant F295A
91
crotonyl-CoA
-
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
92
crotonyl-CoA
-
mutant Y370A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y370A
15.3
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant I287A
19
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L276A/V277A
22.4
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
48
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant Y370A
50
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L291A
64
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant F295A
112
hexanoyl-CoA
-
pH and temperature not specified in the publication, wild-type
2.3
NADH
mutant enzyme Y225A, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant Y225A
16.5
NADH
mutant enzyme F11K, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant F11K
23.6
NADH
mutant enzyme K245A, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant K245A
28.2
NADH
pH 6.2, 25°C, wild-type; wild type enzyme, at pH 6.2 and 25°C
385.9
NADH
-
pH 6.2, 25°C, wild-type; wild type enzyme, at pH 6.2 and 25°C
6
trans-2-dodecenoyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication
24
trans-2-dodecenoyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
90
trans-2-dodecenoyl-CoA
-
wild-type, pH not specified in the publication, temperature not specified in the publication
15.3
trans-2-hexenoyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication
19
trans-2-hexenoyl-CoA
-
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication
22.4
trans-2-hexenoyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
48
trans-2-hexenoyl-CoA
-
mutant Y370A, pH not specified in the publication, temperature not specified in the publication
50
trans-2-hexenoyl-CoA
-
mutant L291A, pH not specified in the publication, temperature not specified in the publication
64
trans-2-hexenoyl-CoA
-
mutant F295A, pH not specified in the publication, temperature not specified in the publication
112
trans-2-hexenoyl-CoA
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
390
NADPH
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2000
2-dodecenoyl-CoA
-
pH and temperature not specified in the publication, mutant I287A
21000
2-dodecenoyl-CoA
-
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
30000
2-dodecenoyl-CoA
-
pH and temperature not specified in the publication, wild-type
15
crotonyl-CoA
-
mutant Y240F, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y240F
40
crotonyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant I287A
89
crotonyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A/F295A
260
crotonyl-CoA
-
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L276A/V277A
300
crotonyl-CoA
-
mutant L291A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant L291A
600
crotonyl-CoA
-
mutant Y370A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant Y370A
700
crotonyl-CoA
-
mutant F295A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, mutant F295A
1300
crotonyl-CoA
-
pH and temperature not specified in the publication, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
1300
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L291A
1500
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L276A/V277A/F295A
2700
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant Y370A
3000
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant L276A/V277A
3400
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant F295A
4500
hexanoyl-CoA
-
pH and temperature not specified in the publication, mutant I287A
9000
hexanoyl-CoA
-
pH and temperature not specified in the publication, wild-type
18
NADH
mutant enzyme Y225A, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant Y225A
180
NADH
mutant enzyme K245A, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant K245A
270
NADH
pH 6.2, 25°C, wild-type; wild type enzyme, at pH 6.2 and 25°C
520
NADH
mutant enzyme F11K, at pH 6.2 and 25°C; pH 6.2, 25°C, mutant F11K
5500
NADH
-
pH 6.2, 25°C, wild-type; wild type enzyme, at pH 6.2 and 25°C
16000
NADH
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2000
trans-2-dodecenoyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication
21000
trans-2-dodecenoyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
30000
trans-2-dodecenoyl-CoA
-
wild-type, pH not specified in the publication, temperature not specified in the publication
1300
trans-2-hexenoyl-CoA
-
mutant L291A, pH not specified in the publication, temperature not specified in the publication
1500
trans-2-hexenoyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
2700
trans-2-hexenoyl-CoA
-
mutant Y370A, pH not specified in the publication, temperature not specified in the publication
3000
trans-2-hexenoyl-CoA
-
mutant L276A/V277A, pH not specified in the publication, temperature not specified in the publication
3400
trans-2-hexenoyl-CoA
-
mutant F295A, pH not specified in the publication, temperature not specified in the publication
4500
trans-2-hexenoyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication
9000
trans-2-hexenoyl-CoA
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
butyryl-CoA
-
pH and temperature not specified in the publication, 0.5 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
0.05
hexanoyl-CoA
-
pH and temperature not specified in the publication, 0.05 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
0.08
hexanoyl-CoA
-
pH and temperature not specified in the publication, 0.25 mM inhibitor, wild-type
0.00003
lauroyl-CoA
-
pH and temperature not specified in the publication, 0.0001 mM inhibitor, mutant I287A
0.00006
lauroyl-CoA
-
mutant I287A, pH not specified in the publication, temperature not specified in the publication; pH and temperature not specified in the publication, 0.00025 mM inhibitor, mutant I287A
0.0004
lauroyl-CoA
-
pH and temperature not specified in the publication, 0.0015 mM inhibitor, wild-type
0.0005
lauroyl-CoA
-
pH and temperature not specified in the publication, 0.001 mM inhibitor, wild-type; wild-type, pH not specified in the publication, temperature not specified in the publication
0.001
lauroyl-CoA
-
mutant L276A/V277A/F295A, pH not specified in the publication, temperature not specified in the publication
0.003
lauroyl-CoA
-
pH and temperature not specified in the publication, 0.010 mM inhibitor, mutant I287A
0.01
lauroyl-CoA
-
pH and temperature not specified in the publication, 0.005 mM inhibitor, mutant I287A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.078
mitochondria, anaerobic conditions, substrates crotonyl-CoA and NADH
0.086
mitochondria, aerobic conditions, substrates crotonyl-CoA and NADH
0.37
purified recombinant enzyme, substrates trans-hexenoyl-CoA and NADPH
1.45
purified recombinant enzyme, substrates trans-hexenoyl-CoA and NADH
3.88
pH 6.2, 30°C; purified native enzyme, substrate crotonyl-CoA and NADH
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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 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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
enzyme is expressed under aerobic and anaerobic conditions
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
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BatG encodes a functional FabI isozyme which confers full resistance to kalimantacin/batumin and complements FabI. BatG is, similarity to trans-2-enoyl-ACP reductases, involved in the formation of a saturated acyl-ACP by an NAD(P)H-dependent reduction of the trans-2-enoyl-ACP double bond, which is essential for the final step of the elongation cycle of fatty acid biosynthesis. BatG knockout does not influence the kalimantacin/batumin, kal/bat, biosynthesis structurally. Kalimantacin/batumin biosynthesis is BatG-independent, despite BatG localization in the operon among kal/bat tailoring enzymes, overview
physiological function
-
BatG encodes a functional FabI isozyme which confers full resistance to kalimantacin/batumin and complements FabI. BatG is, similarity to trans-2-enoyl-ACP reductases, involved in the formation of a saturated acyl-ACP by an NAD(P)H-dependent reduction of the trans-2-enoyl-ACP double bond, which is essential for the final step of the elongation cycle of fatty acid biosynthesis. BatG knockout does not influence the kalimantacin/batumin, kal/bat, biosynthesis structurally. Kalimantacin/batumin biosynthesis is BatG-independent, despite BatG localization in the operon among kal/bat tailoring enzymes, overview
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additional information
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BatG is an isoform of FabI, conferring full resistance to target bacteria against kalimantacin/batumin and/or triclosan
additional information
-
BatG is an isoform of FabI, conferring full resistance to target bacteria against kalimantacin/batumin and/or triclosan
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Show AA Sequence and Transmembrane Helices (544 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
in complex with NAD+, vapor diffusion method; structures of CaTER in apo form at 2.1 A resolution, in complex with NADH at 2.0 A resolution and in complex with NAD+ at 2.7 A resolution
purified and crystallized as an apoenzyme and in a complex form with NADH and triclosan. The crystals of native and complexed FabI diffract to resolutions of 2.6 and 1.8 A, respectively. The crystals both belong to space group P2-1, with unit-cell parameters a = 117.32, b = 155.844, c = 129.448 A , beta = 111.061° for the native enzyme and a = 64.784, b = 107.573, c = 73.517 A, beta = 116.162° for the complex
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crystal structure of tdTer is determined to 2.00 A; to 2.0 A resolution
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in complex with NAD+, vapor diffusion method,; TdTER is crystallized in complex with NAD+ at 3.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F11K
kcat slightly decreased compared to wild-type, Km (NADH) decreased compared to wild-type; the mutant shows 198% activity compared to the wild type enzyme
K245A
kcat slightly decreased compared to wild-type, Km (NADH) increased compared to wild-type; the mutant shows 67 activity compared to the wild type enzyme
Y225A
kcat highly decreased compared to wild-type, Km (NADH) increased compared to wild-type; the mutant shows 6.7 activity compared to the wild type enzyme
K165A
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site-directed mutagenesis, mutation of putative catalytic residue
K165Q
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site-directed mutagenesis, mutation of putative catalytic residue
Y158F
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site-directed mutagenesis, mutation of putative catalytic residue, mutant can only be stably expressed in Escherichia coli strain BL21(DE3) if altered to a soluble enzyme form dependent on IPTG induction
F295A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
I287A
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mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type
L276A/V277A
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mutant shows significant decreased kcat values compared to wild-type
L276A/V277A/F295A
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mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket
L291A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
Y240F
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Y240F mutation leads to a 5000fold decrease in catalytic efficiency compared to wild-type with no significant change in Km
Y370A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
F295A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
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I287A
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mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type
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L291A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
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Y240F
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Y240F mutation leads to a 5000fold decrease in catalytic efficiency compared to wild-type with no significant change in Km
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Y370A
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mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
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additional information
additional information
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construction of stable mutants for optimization of expression of enzyme in Escherichia coli, absolutely dependent on IPTG, phenotype alterations, overview
additional information
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generation of a specific in vivo gene inactivation by in-frame deletion of BatG
additional information
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generation of a specific in vivo gene inactivation by in-frame deletion of BatG
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
; native enzyme 1687fold to homogeneity in several steps, recombinant His-tagged enzyme from Escherichia coli by affinity chromatography
purified by gel-filtration chromatography on a HiLoad 16/60 superdex 200 column
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using Ni-NTA chromatography
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
gene inhA, overexpression of stable mutant enzymes in Escherichia coli strain BL21(DE3)
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phage library screening, DNA and amino acid sequence determination and analysis, phylogenetic analysis, functional expression as His-tagged enzyme in Escherichia coli
wild-type and deletion mutant BatG expression in Pseudomonas fluorescens strain BCCM_ID9359, Escherichia coli, and Staphylococcus aureus, confers resistance against kalimantacin/batumin
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expressed in Escherichia coli as a His-tagged fusion protein
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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enzyme is a target for drugs in treatment of tuberculosis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Miller, T.L.; Jenesel, S.E.
Enzymology of butyrate formation by Butyrivibrio fibrisolvens
J. Bacteriol.
138
99-104
1979
Butyrivibrio fibrisolvens
brenda
Nagi, M.N.; Prasad, M.R.; Cook, L.; Cinti, D.
Biochemical properties of short- and long-chain rat liver microsomal trans-2-enoyl coenzyme A reductase
Arch. Biochem. Biophys.
226
50-64
1983
Rattus norvegicus
brenda
Prasad, M.R.; Nagi, M.N.; Cook, L.; Cinti, D.L.
Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase
Biochem. Biophys. Res. Commun.
113
659-665
1983
Rattus norvegicus
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Purification and some properties of short chain-length specific trans-2-enoyl-CoA reductase in mitochondria of Euglena gracilis
J. Biochem.
100
995-1000
1986
Euglena gracilis
brenda
Shimakata, T.; Kusaka, T.
Purification and characterization of 2-enoyl-CoA reductase of Mycobacterium smegmatis
J. Biochem.
89
1075-1080
1981
Mycolicibacterium smegmatis
brenda
Shimakata, T.; Fujita, Y.; Kusaka, T.
Involvement of one of two enoyl-CoA hydratases and enoyl-CoA reductase in the acetyl-CoA-dependent elongation of medium chain fatty acids by Mycobacterium smegmatis
J. Biochem.
88
1051-1058
1980
Mycolicibacterium smegmatis
brenda
Inui, H.; Miyatake, K.; Nakano, Y.; Kitaoka, S.
Fatty acid synthesis in mitochondria of Euglena gracilis
Eur. J. Biochem.
142
121-126
1984
Euglena gracilis
brenda
Hoffmeister, M.; Piotrowski, M.; Nowitzki, U.; Martin, W.
Mitochondrial trans-2-enoyl-CoA reductase of wax ester fermentation from Euglena gracilis defines a new family of enzymes involved in lipid synthesis
J. Biol. Chem.
280
4329-4338
2005
Euglena gracilis (Q5EU90)
brenda
Poletto, S.S.; da Fonseca, I.O.; de Carvalho, L.P.; Basso, L.A.; Santos, D.S.
Selection of an Escherichia coli host that expresses mutant forms of Mycobacterium tuberculosis 2-trans enoyl-ACP(CoA) reductase and 3-ketoacyl-ACP(CoA) reductase enzymes
Protein Expr. Purif.
34
118-125
2004
Mycobacterium tuberculosis
brenda
Tucci, S.; Martin, W.
A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete Treponema denticola
FEBS Lett.
581
1561-1566
2007
Treponema denticola
brenda
Mattheus, W.; Masschelein, J.; Gao, L.J.; Herdewijn, P.; Landuyt, B.; Volckaert, G.; Lavigne, R.
The kalimantacin/batumin biosynthesis operon encodes a self-resistance isoform of the FabI bacterial target
Chem. Biol.
17
1067-1071
2010
Pseudomonas fluorescens, Pseudomonas fluorescens BCCM_ID9359
brenda
Lee, J.H.; Park, A.K.; Chi, Y.M.; Moon, J.H.; Lee, K.S.
Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
67
214-216
2011
Pseudomonas aeruginosa
brenda
Hu, K.; Zhao, M.; Zhang, T.; Zha, M.; Zhong, C.; Jiang, Y.; Ding, J.
Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum and Treponema denticola: insights into the substrate specificity and the catalytic mechanism
Biochem. J.
449
79-89
2013
Clostridium acetobutylicum, Clostridium acetobutylicum (Q97LU2), Treponema denticola (Q73Q47), Treponema denticola, Treponema denticola ATCC 35405
brenda
Bond-Watts, B.B.; Weeks, A.M.; Chang, M.C.
Biochemical and structural characterization of the trans-enoyl-CoA reductase from Treponema denticola
Biochemistry
51
6827-6837
2012
Treponema denticola (Q73Q47), Treponema denticola, Treponema denticola ATCC 35405 (Q73Q47)
brenda
Schadeweg, V.; Boles, E.
Increasing n-butanol production with Saccharomyces cerevisiae by optimizing acetyl-CoA synthesis, NADH levels and trans-2-enoyl-CoA reductase expression
Biotechnol. Biofuels
9
257
2016
Treponema denticola, Treponema denticola VSY0
brenda
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