PMID:2015910

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Citation

Kessler, D, Leibrecht, I and Knappe, J (1991) Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE. FEBS Lett. 281:59-63

Abstract

A 4.8 kb DNA-fragment was cloned and sequenced encompassing the structural gene of PFL-deactivase (2.7 kb) and 2 kb of the 5' flanking region that contains the elements for anaerobic induction. A mutant lacking deactivase was shown to require exogenous electron acceptors for anaerobic growth with glucose. This revealed the identity of PFL-deactivase with the alcohol and acetaldehyde dehydrogenases of E. coli. The multienzyme represents a homopolymeric protein (approximately 40 x 96 kDa) requiring Fe2+ for all functions.

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Keywords

Alcohol Dehydrogenase/genetics; Alcohol Dehydrogenase/isolation & purification; Alcohol Dehydrogenase/metabolism; Aldehyde Oxidoreductases/genetics; Aldehyde Oxidoreductases/isolation & purification; Aldehyde Oxidoreductases/metabolism; Anaerobiosis; Base Sequence; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Escherichia coli Proteins; Genes, Bacterial; Kinetics; Molecular Sequence Data; Multienzyme Complexes/genetics; Multienzyme Complexes/isolation & purification; Multienzyme Complexes/metabolism; Plasmids; Restriction Mapping

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