PMID:8119879
| Citation |
Bergler, H, Wallner, P, Ebeling, A, Leitinger, B, Fuchsbichler, S, Aschauer, H, Kollenz, G, Högenauer, G and Turnowsky, F (1994) Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli. J. Biol. Chem. 269:5493-6 |
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| Abstract |
The EnvM protein was purified from an overproducing Escherichia coli strain. It showed NADH-dependent enoyl-acyl carrier protein (ACP) reductase activity using both crotonyl-ACP and crotonyl-CoA as substrates. The protein bound a radioactive diazaborine derivative in the presence of NAD+ and radioactive NAD+ in the presence of the drug. Based on these data, it is concluded that EnvM is the NADH-dependent enoyl-ACP reductase (EC 1.3.1.9) of E. coli and we propose to rename the corresponding gene fabI. |
| Links | |
| Keywords |
Acyl Coenzyme A/metabolism; Amino Acid Sequence; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Carrier Proteins/metabolism; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Enoyl-(Acyl-Carrier-Protein) Reductase (NADH); Escherichia coli/enzymology; Escherichia coli Proteins; Fatty Acid Synthetase Complex, Type II; Kinetics; Molecular Sequence Data; NAD/metabolism; Oxidoreductases/metabolism; Pharmaceutical Preparations/metabolism; Sequence Homology, Amino Acid |
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