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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acyl Coenzyme A / metabolism
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Amino Acid Sequence
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Carrier Proteins / metabolism
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Chromatography, Ion Exchange
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Electrophoresis, Polyacrylamide Gel
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Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
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Escherichia coli / enzymology*
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Escherichia coli Proteins
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Fatty Acid Synthase, Type II
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Kinetics
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Molecular Sequence Data
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NAD / metabolism
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Oxidoreductases / metabolism*
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Pharmaceutical Preparations / metabolism
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Sequence Homology, Amino Acid
Substances
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Acyl Coenzyme A
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Bacterial Proteins
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Carrier Proteins
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Escherichia coli Proteins
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Pharmaceutical Preparations
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NAD
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crotonyl-coenzyme A
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Oxidoreductases
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Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
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fabI protein, E coli
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Fatty Acid Synthase, Type II