Protein EnvM is the NADH-dependent enoyl-ACP reductase (FabI) of Escherichia coli

J Biol Chem. 1994 Feb 25;269(8):5493-6.


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 of E. coli and we propose to rename the corresponding gene fabI.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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 Synthase, Type II
  • Kinetics
  • Molecular Sequence Data
  • NAD / metabolism
  • Oxidoreductases / metabolism*
  • Pharmaceutical Preparations / metabolism
  • Sequence Homology, Amino Acid


  • Acyl Coenzyme A
  • Bacterial Proteins
  • Carrier Proteins
  • Escherichia coli Proteins
  • Pharmaceutical Preparations
  • NAD
  • crotonyl-coenzyme A
  • Oxidoreductases
  • Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
  • fabI protein, E coli
  • Fatty Acid Synthase, Type II