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(E)-2-hexanoyl-CoA + NADPH
hexanoyl-CoA + NADP+
2-decenoyl-CoA + NADH + H+
decanoyl-CoA + NAD+
-
-
-
-
r
2-hexadecenoyl-CoA + NADH + H+
hexadecanoyl-CoA + NAD+
-
-
-
-
r
acyl-CoA + NAD+
trans-2,3-didehydroacyl-CoA + NADH
crotonyl-CoA + NAD(P)H
butyryl-CoA + NAD(P)+
-
-
-
?
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
crotonyl-CoA + NADH
butyryl-CoA + NAD+
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
dodec-2-enoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
-
-
-
-
r
hexenoyl-CoA + NADH
? + NAD+
trans-2-decenoyl-CoA + NADH
decanoyl-CoA + NAD+
trans-2-dodecenoyl-CoA + NADH
dodecanoyl-CoA + NAD+
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)+
trans-2-hexenoyl-CoA + NADH + H+
hexanoyl-CoA + NAD+
-
-
-
?
trans-2-octenoyl-CoA + NADH
octanoyl-CoA + NAD+
trans-didehydroacyl-CoA + NAD(P)H
acyl-CoA + NAD(P)+
i.e. enoyl-CoA
-
-
?
additional information
?
-
(E)-2-hexanoyl-CoA + NADPH
hexanoyl-CoA + NADP+
-
-
-
?
(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+
-
-
-
?, ir
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
-
-
-
-
ir
crotonyl-CoA + NADH
butanoyl-CoA + NAD+
-
-
-
ir
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
butyryl-CoA + NAD+
-
reductase I highest activity
-
-
?
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 + NADH + H+
butyryl-CoA + NAD+
-
-
-
r
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
-
-
-
-
?
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
-
-
-
?
crotonyl-CoA + NADH + H+
butyryl-CoA + NAD+
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-CoA + NADPH
butanoyl-CoA + NADP+
-
-
-
?
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-decenoyl-CoA + NADH
decanoyl-CoA + NAD+
-
-
-
-
?
trans-2-dodecenoyl-CoA + NADH
dodecanoyl-CoA + NAD+
-
-
-
-
?
trans-2-dodecenoyl-CoA + NADH
dodecanoyl-CoA + NAD+
-
-
i.e. laurate
?
trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
-
-
-
?
trans-2-dodecenoyl-CoA + NADH + H+
dodecanoyl-CoA + NAD+
-
-
-
?
trans-2-hexadecenoyl-CoA + NADH
hexadecanoyl-CoA + NAD+
-
-
-
-
?
trans-2-hexadecenoyl-CoA + NADH
hexadecanoyl-CoA + NAD+
-
-
-
-
?
trans-2-hexenoyl-CoA + NAD(P)H
hexanoyl-CoA + NAD(P)+
-
-
-
?
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
-
-
?
trans-2-octenoyl-CoA + NADH
octanoyl-CoA + NAD+
-
-
-
-
?
trans-2-octenoyl-CoA + NADH
octanoyl-CoA + NAD+
-
-
-
-
?
additional information
?
-
no activity with butanoyl-CoA
-
-
?
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
?
-
-
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
-
-
?
additional information
?
-
-
long-chain substrates preferred
-
-
?
additional information
?
-
-
not active with NADPH or hexenoyl-CoA
-
-
?
additional information
?
-
-
no activity with butanoyl-CoA
-
-
?
additional information
?
-
no activity with butanoyl-CoA
-
-
?
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0.2327
(2E)-oct-2-enoyl-CoA
-
-
0.0893
2-decenoyl-CoA
-
-
0.004
2-dodecenoyl-CoA
pH and temperature not specified in the publication, mutant I287A
0.0027
crotonoyl-CoA
-
in potassium phosphate buffer pH 6.2, at 30°C
0.049 - 0.21
crotonyl-CoA
0.0558
dodec-2-enoyl-CoA
-
-
0.0295
hexadecenoyl-CoA
-
-
0.0034 - 0.038
hexanoyl-CoA
0.0011 - 0.004
trans-2-dodecenoyl-CoA
0.0034 - 0.091
trans-2-hexenoyl-CoA
0.109
Biochanin A
recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate
0.109
Biochanin A
cosubstrate crotonyl-CoA, pH 6.2, 30°C
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
pH 6.2, 30°C
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
0.0316
NADH
pH 6.2, 25°C, mutant F11K
0.0316
NADH
mutant enzyme F11K, at pH 6.2 and 25°C
0.0697
NADH
wild type enzyme, at pH 6.2 and 25°C
0.1054
NADH
wild type enzyme, at pH 6.2 and 25°C
0.129
NADH
pH 6.2, 25°C, mutant Y225A
0.1299
NADH
mutant enzyme Y225A, at pH 6.2 and 25°C
0.132
NADH
pH 6.2, 25°C, mutant K245A
0.1323
NADH
mutant enzyme K245A, at pH 6.2 and 25°C
0.119
NADPH
recombinant enzyme, pH 6.2, 30°C, with crotonyl-CoA as substrate
0.119
NADPH
cosubstrate crotonyl-CoA, pH 6.2, 30°C
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
0.091
trans-2-hexenoyl-CoA
recombinant enzyme, pH 6.2, 30°C, with NADH as cofactor
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6 - 90
trans-2-dodecenoyl-CoA
15.3 - 112
trans-2-hexenoyl-CoA
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
91
crotonyl-CoA
pH and temperature not specified in the publication, wild-type
92
crotonyl-CoA
mutant Y370A, pH not specified in the publication, temperature not specified in the publication
92
crotonyl-CoA
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
pH 6.2, 25°C, mutant Y225A
2.3
NADH
mutant enzyme Y225A, at pH 6.2 and 25°C
16.5
NADH
pH 6.2, 25°C, mutant F11K
16.5
NADH
mutant enzyme F11K, at pH 6.2 and 25°C
23.6
NADH
pH 6.2, 25°C, mutant K245A
23.6
NADH
mutant enzyme K245A, at pH 6.2 and 25°C
28.2
NADH
pH 6.2, 25°C, wild-type
28.2
NADH
wild type enzyme, at pH 6.2 and 25°C
385.9
NADH
pH 6.2, 25°C, wild-type
385.9
NADH
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.
2000 - 30000
2-dodecenoyl-CoA
390
NADPH
wild-type, pH not specified in the publication, temperature not specified in the publication
2000 - 30000
trans-2-dodecenoyl-CoA
1300 - 9000
trans-2-hexenoyl-CoA
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
15
crotonyl-CoA
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
40
crotonyl-CoA
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
89
crotonyl-CoA
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
260
crotonyl-CoA
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
300
crotonyl-CoA
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
600
crotonyl-CoA
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
700
crotonyl-CoA
pH and temperature not specified in the publication, mutant F295A
1300
crotonyl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication
1300
crotonyl-CoA
pH and temperature not specified in the publication, wild-type
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
pH 6.2, 25°C, mutant Y225A
18
NADH
mutant enzyme Y225A, at pH 6.2 and 25°C
180
NADH
pH 6.2, 25°C, mutant K245A
180
NADH
mutant enzyme K245A, at pH 6.2 and 25°C
270
NADH
pH 6.2, 25°C, wild-type
270
NADH
wild type enzyme, at pH 6.2 and 25°C
520
NADH
pH 6.2, 25°C, mutant F11K
520
NADH
mutant enzyme F11K, at pH 6.2 and 25°C
5500
NADH
pH 6.2, 25°C, wild-type
5500
NADH
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.
0.000198
crotonoyl-CoA
-
in potassium phosphate buffer pH 6.2, at 30°C
0.00003 - 0.01
lauroyl-CoA
0.4
butyryl-CoA
wild-type, pH not specified in the publication, temperature not specified in the publication
0.4
butyryl-CoA
pH and temperature not specified in the publication, 0.5 mM inhibitor, wild-type
0.05
hexanoyl-CoA
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
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
0.00006
lauroyl-CoA
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
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0005
lauroyl-CoA
pH and temperature not specified in the publication, 0.001 mM inhibitor, wild-type
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
the enzyme (EgTER1) is involved in the greening process. It is dispensable for wax ester production under anaerobic conditions
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
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BatG is an isoform of FabI, conferring full resistance to target bacteria against kalimantacin/batumin and/or triclosan
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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
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
I287A
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
mutant shows significant decreased kcat values compared to wild-type
L276A/V277A/F295A
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
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA
Y240F
Y240F mutation leads to a 5000fold decrease in catalytic efficiency compared to wild-type with no significant change in Km
Y370A
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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F11K
kcat slightly decreased compared to wild-type, Km (NADH) decreased compared to wild-type
F11K
the mutant shows 198% activity compared to the wild type enzyme
K244A
inactive
K244A
mutant shows no activity
K245A
kcat slightly decreased compared to wild-type, Km (NADH) increased compared to wild-type
K245A
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
Y225A
the mutant shows 6.7 activity compared to the wild type enzyme
Y235F
inactive
Y235F
mutant shows no activity
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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Miller, T.L.; Jenesel, S.E.
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17
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Pseudomonas fluorescens, Pseudomonas fluorescens BCCM_ID9359
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Crystallization and preliminary X-ray crystallographic studies of enoyl-acyl carrier protein reductase (FabI) from Pseudomonas aeruginosa
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67
214-216
2011
Pseudomonas aeruginosa
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Hu, K.; Zhao, M.; Zhang, T.; Zha, M.; Zhong, C.; Jiang, Y.; Ding, J.
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Biochemical and structural characterization of the trans-enoyl-CoA reductase from Treponema denticola
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Treponema denticola (Q73Q47), Treponema denticola, Treponema denticola ATCC 35405 (Q73Q47)
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Increasing n-butanol production with Saccharomyces cerevisiae by optimizing acetyl-CoA synthesis, NADH levels and trans-2-enoyl-CoA reductase expression
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A major isoform of mitochondrial trans-2-enoyl-CoA reductase is dispensable for wax ester production in Euglena gracilis under anaerobic conditions
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Euglena gracilis (Q5EU90), Euglena gracilis
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