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(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
1-cyclohexenylcarbonyl-CoA + NADPH
1-cyclohexylcarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
2-decenoyl-[acyl-carrier protein] + NADPH
decanoyl-[acyl-carrier protein] + NADP+
-
syn addition of hydrogen via a 2-Re,3-Si attack on the double bond
-
?
2-hexenoyl-[acyl-carrier protein] + NADPH
hexanoyl-[acyl-carrier protein] + NADP+
2-trans-hexenoyl-CoA + NADPH
?
-
assay at pH 7.5, 23°C
-
-
?
5-hydroxycyclohex-1-enecarbonyl-CoA + NADPH
5-hydroxycyclohexylcarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
beta-ketoacyl-[acyl-carrier protein] + NADH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NAD+
-
-
-
-
?
crotonyl-CoA + NADPH + H+
?
crotonyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
-
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
crotonyl-N-acetyl-cysteamine + NADPH + H+
butyryl-N-acetyl-cysteamine + NADP+
-
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
crotonyl-[acyl-carrier protein] + NADPH + H+
?
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
crotonyl-[Staphylococcus aureus acyl carrier protein] + NADPH + H+
butyryl-[Staphylococcus aureus acyl carrier protein] + NADP+
-
-
-
-
?
dodec-2-enoyl-CoA + NADPH + H+
dodecanoyl-CoA + NADP+
-
-
-
-
r
dodecenoyl-CoA + NADPH + H+
dodecanoyl-CoA + NADP+
-
-
-
-
?
dodecenoyl-N-acetyl-cysteamine + NADPH + H+
dodecanoyl-N-acetyl-cysteamine + NADP+
-
-
-
-
?
dodecenoyl-[Staphylococcus aureus acyl carrier protein] + NADPH + H+
dodecanoyl-[Staphylococcus aureus acyl carrier protein] + NADP+
-
-
-
-
?
hexanoyl-CoA + NADH + H+
?
-
-
-
-
?
hexanoyl-[acyl-carrier protein] + NADH + H+
?
-
-
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
acyl-[acyl-carrier protein] + NADP+
-
prefers acyl carrier protein substrates carrying fatty acids with long acyl chains
-
-
?
trans-2-hexenoyl-CoA + NADPH
hexanoyl-CoA + NADP+
-
-
-
-
?
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA + NADPH
trans-4,5-dihydroxycyclohexa-2-enecarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
additional information
?
-
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
-
-
-
?
(2E)-but-2-enoyl-[acyl carrier protein] + NADPH + H+
butanoyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
2-hexenoyl-[acyl-carrier protein] + NADPH
hexanoyl-[acyl-carrier protein] + NADP+
-
-
-
?
2-hexenoyl-[acyl-carrier protein] + NADPH
hexanoyl-[acyl-carrier protein] + NADP+
-
-
-
?
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
-
?
acyl-[acyl-carrier protein] + NADP+
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
assay method by consumption of beta-nicotinamide adenine dinucleotide phosphate during reduction of trans-2-octenoyl-N-acetylcysteamine as the substrate
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
?
crotonyl-CoA + NADPH + H+
?
-
-
-
-
?
crotonyl-CoA + NADPH + H+
?
-
-
-
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
-
stereochemistry
-
?
crotonyl-N-acetyl-cysteamine + NADPH
butyryl-N-acetyl-cysteamine + NADP+
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
anti addition of hydrogen via a 2-Si,3-Si attack on the double bond
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
anti addition of hydrogen via a 2-Si,3-Si attack on the double bond
-
?
crotonyl-[acyl-carrier protein] + NADPH
butyryl-[acyl-carrier protein] + NADP+
-
substrate created by E. coli enzymes during assay
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
?
-
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
?
-
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
-
-
-
?
crotonyl-[acyl-carrier protein] + NADPH + H+
butyryl-[acyl-carrier protein] + NADP+
-
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
-
-
?
octenoyl-N-acetyl-cysteamine + NADPH
octanoyl-N-acetyl-cysteamine + NADP+
-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
-
-
-
?
S-((2E)-oct-2-enoyl)-N-acetylcysteamine + NADPH + H+
S-octanoyl-N-acetylcysteamine + NADP+
-
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
-
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
-
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
active on substrates with acyl chain length C4-C16
-
-
?
additional information
?
-
-
active on substrates with acyl chain length C4-C16
-
-
?
additional information
?
-
-
inactive with enoyl-CoA substrates
-
-
?
additional information
?
-
-
inactive with enoyl-CoA substrates
-
-
?
additional information
?
-
-
inactive with enoyl-CoA substrates
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
enzyme possesses intrinsic NADPH oxidase activity in the absence of the crotonyl-CoA substrate
-
-
?
additional information
?
-
-
enzyme possesses intrinsic NADPH oxidase activity in the absence of the crotonyl-CoA substrate
-
-
?
additional information
?
-
enzyme possesses intrinsic NADPH oxidase activity in the absence of the crotonyl-CoA substrate
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
no activity with crotonyl-CoA and NADH
-
-
?
additional information
?
-
-
activity measurement by reduction of the trans-2-octenoyl N-acetylcysteamine as substrate and NADPH as cofactor
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
the purified protein exhibits NADPH-dependent enoyl-acyl carrier protein reductases activity but no 7alpha-hydroxysteroid dehydrogenase activity, despite its high homology with 7-AHSDH
-
-
-
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1-cyclohexenylcarbonyl-CoA + NADPH
1-cyclohexylcarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
5-hydroxycyclohex-1-enecarbonyl-CoA + NADPH
5-hydroxycyclohexylcarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
beta-ketoacyl-[acyl-carrier protein] + NADH + H+
beta-hydroxyacyl-[acyl-carrier protein] + NAD+
-
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA + NADPH
trans-4,5-dihydroxycyclohexa-2-enecarbonyl-CoA + NADP+
-
reaction in ansatrienin biosynthesis out of shikimic acid
-
?
additional information
?
-
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
-
?
an acyl-[acyl-carrier protein] + NADP+
a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH + H+
-
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
-
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH
acyl-[acyl-carrier protein] + NADP+
reaction within the fatty acid synthase complex, indispensable for respiratory function in mitochondria
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
-
catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters of both N-acetylcysteamine and acyl-carrier protein
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
additional information
?
-
-
part of fatty acid synthesis reducing double bonds of a great varity of acyl thioesters
-
-
?
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0.025
1-cyclohexenylcarbonyl-CoA
-
vmax 0.0075 mmol/mg/min
0.03
5-hydroxycyclohex-1-enecarbonyl-CoA
-
vmax 0.0053 mmol/mg/min
0.00963
crotonyl-CoA
pH 7.0, 25°C
0.008 - 8
Crotonyl-N-acetyl-cysteamine
0.0478
crotonyl-[acyl-carrier protein]
pH 7.5, 25°C
0.0115
crotonyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0241
dodec-2-enoyl-CoA
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0233
dodecenoyl-N-acetyl-cysteamine
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0045 - 0.0184
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
additional information
NADPH
0.008
Crotonyl-N-acetyl-cysteamine
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
8
Crotonyl-N-acetyl-cysteamine
Vmax 0.0003 nmol/min/mg
0.0045
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0114
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme A95V, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.0184
dodecenoyl-[Staphylococcus aureus acyl carrier protein]
-
mutant enzyme F204S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.016
NADPH
-
0.016
NADPH
no cooperativity in binding NADPH
0.0171
NADPH
pH 7.5, 25°C
0.0276
NADPH
pH 7.0, 25°C
0.2694
NADPH
-
mutant enzyme A95V, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
0.4296
NADPH
-
mutant enzyme F204S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
1
NADPH
-
Km above 1 mM, mutant enzyme I193S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)
additional information
NADPH
-
value above 2 mM
additional information
NADPH
half-maximal rate at 0.065 mM NADPH
additional information
NADPH
-
half-maximal rate at 0.065 mM NADPH
additional information
NADPH
cooperative binding with Hill coefficient 2.2
additional information
NADPH
-
cooperative binding with Hill coefficient 2.2
additional information
trans-3,4-dihydroxycyclohexa-1,5-dienecarbonyl-CoA
-
only impure solution available, KM and vmax in same order of magnitude as with 1-cyclohexenylcarbonyl-CoA
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FabL in apo form and in the ternary complex with NADP+ and an indole naphthyridinone inhibitor, X-ray diffraction structure determination and analysis
FabL in apo form and in the ternary complex with NADP+ and inhibitor (E)-N-(1,2-dimethyl-1-H-indol-3-ylmethyl)-N-methyl-3-(7-oxo-5,6,7,8-tetrahydro-1,8-naphthyridin-3-yl) acrylamide, 8 mg/ml protein in 20 mM Tris, pH 8.0, 100 mM NaCl, and 1 mM DTT, is mixed with an equal volume of reservoir solution containing 0.1 M sodium citrate pH 5.6, 8% w/v PEG 10,000 and 0.4 M magnesium acetate, hanging-drop methods, for the ternary BcFabL-NADP+-INH complex, NADP+ and inhibitor are added at the molar ratio of 1:1.5 and 1:5, respectively, equilibration in a stabilizing solution containing 0.1 M sodium citrate, pH 5.6, 8% w/v PEG 10,000, 0.4 M magnesium acetate with 30% v/v ethylene glycol as the cryoprotectant, X-ray diffraction structure determination and analysis at 2.2-3.0 A resolution
hanging drop vapour diffusion method with 0.04 M MgCl2, 0.05 M sodium cacodylate pH 6.0 and 11% (v/v) 2-methyl-2,4-pentanediol at 4°C
-
purified recombinant wild-type enzyme free and in complex with NADPH, mutant enzyme Y79N, hanging drop vapour diffusion method, 22°C, 15-25 mg/ml free enzyme in 50 mM sodium phosphate, pH 7.0, 150 mM NaCl with or without 10 mM NADPH, in a 1:1 ratio with reservoir solution containing 1.9 M ammonium sulfate, and 0.1 M N-(2-acetamido)-2-iminodiacetic acid/NaOH, at pH 6.5 for the free enzyme and pH 7.0 for the cofactor-complexed enzyme, mutant Y79N is crystallized using 15 mg/ml protein and reservoir solution at pH 7.0, labeling by soaking in heavy-atom-solutions, X-ray diffraction structure determination and analysis at 1.7 A, 2.25 A, and 2.6 A, respectively
-
structure to 1.9 A resolution with endogenous FMN fully resolved and the NADPH cofactor partially resolved. FabK possesses a TIM-barrel motif, and all flexible loops are visible
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Shimakata, T.; Stumpf, P.K.
The procaryotic nature of the fatty acid synthetase of developing Carthamus tinctorius L. (Safflower) seeds
Arch. Biochem. Biophys.
217
144-154
1982
Carthamus tinctorius
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Saito, K.; Kawaguchi, A.; Seyama, Y.; Yamakawa, T.; Okuda, S.
Steric course of reaction catalyzed by the enoyl acyl-carrier-protein reductase of Escherichia coli
Eur. J. Biochem.
116
581-586
1981
Escherichia coli
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Sedgwick, B.; Morris, C.
Stereochemical course of hydrogen transfer catalysed be the enoyl reductase enzyme of the yeast fatty acid synthethase
J. Chem. Soc. Chem. Commun.
1980
96-97
1980
Saccharomyces cerevisiae
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Seyama, Y.; Kasama, T.; Yamakawa, T.; Kawaguchi, A.; Saito, K.; Okuda, S.
Origin of hydrogen atoms in the fatty acids synthesized with yeast fatty acid synthetase
J. Biochem.
82
1325-1329
1977
Saccharomyces cerevisiae, Escherichia coli
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Weeks, G.; Wakil, S.J.
Enoyl acyl carrier protein reductase from Escherichia coli
Methods Enzymol.
14
66-73
1969
Escherichia coli
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Weeks, G.; Wakil, S.J.
Studies on the mechanism of fatty acid synthesis. 18. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli
J. Biol. Chem.
243
1180-1189
1968
Escherichia coli
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Saito, K.; Kawaguchi, A.; Okuda, S.; Seyama, Y.; Yamakawa, T.
Incorporation of hydrogen atoms from deuterated water and stereospecifically deuterium-labeled nicotin amide nucleotides into fatty acids with the Escherichia coli fatty acid synthetase system
Biochim. Biophys. Acta
618
202-213
1980
Escherichia coli
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Bergler, H.; Fuchsbichler, S.; Hoegenauer, G.; Turnowsky, F.
The enoyl-[acyl-carrier-protein] reductase (FabI) of Escherichia coli, which catalyzes a key regulatory step in fatty acid biosynthesis, accepts NADH and NADPH as cofactors and is inhibited by palmitoyl-CoA
Eur. J. Biochem.
242
689-694
1996
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
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Heath, R.J.; Li, J.; Roland, G.E.; Rock, C.O.
Inhibition of the Staphylococcus aureus NADPH-dependent enoyl-acyl carrier protein reductase by triclosan and hexachlorophene
J. Biol. Chem.
275
4654-4659
2000
Escherichia coli, Staphylococcus aureus (Q9RMI3), Staphylococcus aureus
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Heath, R.J.; Su, N.; Murphy, C.K.; Rock, C.O.
The enoyl-[acyl-carrier-protein] reductases FabI and FabL from Bacillus subtilis
J. Biol. Chem.
275
40128-40133
2000
Bacillus subtilis, Bacillus subtilis (P71079)
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Turnowsky, F.; Fuchs, K.; Jeschek, C.; Hogenauer, G.
EnvM genes of Salmonella typhimurium and Escherichia coli
J. Bacteriol.
171
6555-6565
1989
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
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Bergler, H.; Hogenauer, G.; Turnowsky, F.
Sequences of the envM gene and of two mutated alleles in Escherichia coli
J. Gen. Microbiol.
138
2093-2100
1992
Escherichia coli
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Heath, R.J.; Rock, C.O.
A triclosan-resistant bacterial enzyme
Nature
406
145-146
2000
Streptococcus pneumoniae
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Wang, P.; Denoya, C.D.; Morgenstern, M.R.; Skinner, D.D.; Kimberlee, K.W.; Digate, R.; Patton, S.; Banavali, N.; Schuler, G.; Speedie, M.K.; Reynolds, K.A.
Cloning and characterization of the gene encoding 1-cyclohexenylcarbonyl coenzyme A reductase from Streptomyces collinus
J. Bacteriol.
178
6873-6881
1996
Streptomyces collinus
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Airenne, T.T.; Torkko, J.M.; Van den plas, S.; Sormunen, R.T.; Kastaniotis, A.J.; Wierenga, R.K.; Kalervo Hiltunen, J.
Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance
J. Mol. Biol.
327
47-59
2003
Candida tropicalis, Saccharomyces cerevisiae (P38071), Saccharomyces cerevisiae
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Kim, K.H.; Park, J.K.; Ha, B.H.; Moon, J.H.; Kim, E.E.
Crystallization and preliminary X-ray crystallographic analysis of enoyl-ACP reductase III (FabL) from Bacillus subtilis
Acta Crystallogr. Sect. F
63
246-248
2007
Bacillus subtilis, Bacillus subtilis 168
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Xu, H.; Sullivan, T.J.; Sekiguchi, J.; Kirikae, T.; Ojima, I.; Stratton, C.F.; Mao, W.; Rock, F.L.; Alley, M.R.; Johnson, F.; Walker, S.G.; Tonge, P.J.
Mechanism and inhibition of saFabI, the enoyl reductase from Staphylococcus aureus
Biochemistry
47
4228-4236
2008
Staphylococcus aureus
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Gurvitz, A.
A novel circuit overrides Adr1p control during expression of Saccharomyces cerevisiae 2-trans-enoyl-ACP reductase Etr1p of mitochondrial type 2 fatty acid synthase
FEMS Microbiol. Lett.
297
255-260
2009
Saccharomyces cerevisiae
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Kim, S.J.; Ha, B.H.; Kim, K.H.; Hong, S.K.; Shin, K.J.; Suh, S.W.; Kim, E.E.
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus
Biochem. Biophys. Res. Commun.
400
517-522
2010
Bacillus cereus, Bacillus cereus (Q81GI3), Bacillus cereus 6A5, Bacillus cereus DSM 31 (Q81GI3)
brenda
Kwon, Y.J.; Fang, Y.; Xu, G.H.; Kim, W.G.
Aquastatin A, a new inhibitor of enoyl-acyl carrier protein reductase from Sporothrix sp. FN611
Biol. Pharm. Bull.
32
2061-2064
2009
Staphylococcus aureus
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Hevener, K.E.; Mehboob, S.; Boci, T.; Truong, K.; Santarsiero, B.D.; Johnson, M.E.
Expression, purification and characterization of enoyl-ACP reductase II, FabK, from Porphyromonas gingivalis
Protein Expr. Purif.
85
100-108
2012
Porphyromonas gingivalis (Q7MAW0), Porphyromonas gingivalis, Porphyromonas gingivalis W83 (Q7MAW0)
brenda
Dutta, D.; Bhattacharyya, S.; Roychowdhury, A.; Biswas, R.; Das, A.
Crystal structure of hexanoyl-CoA bound to beta-ketoacyl reductase FabG4 of Mycobacterium tuberculosis
Biochem. J.
450
127-139
2013
Mycobacterium tuberculosis
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Yao, J.; Maxwell, J.B.; Rock, C.O.
Resistance to AFN-1252 arises from missense mutations in Staphylococcus aureus enoyl-acyl carrier protein reductase (FabI)
J. Biol. Chem.
288
36261-36271
2013
Staphylococcus aureus, Staphylococcus aureus RN4220
brenda
Hevener, K.; Santarsiero, B.; Lee, H.; Jones, J.; Boci, T.; Johnson, M.; Mehboob, S.
Structural characterization of Porphyromonas gingivalis enoyl-ACP reductase II (FabK)
Acta Crystallogr. Sect. F
74
105-112
2018
Porphyromonas gingivalis (Q7MAW0), Porphyromonas gingivalis, Porphyromonas gingivalis ATCC BAA-308 (Q7MAW0)
brenda
Khan, R.; Zeb, A.; Roy, N.; Magar, R.; Kim, H.; Lee, K.; Lee, S.
Biochemical and structural basis of triclosan resistance in a novel enoyl-acyl carrier protein reductase
Antimicrob. Agents Chemother.
62
e00648
2018
uncultured bacterium pBF1 (A0A1C9U547)
brenda