Pyruvate-formate-lyase-deactivase and acetyl-CoA r...[FEBS Lett. 1991]

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1: FEBS Lett. 1991 Apr 9;281(1-2):59-63. Links

Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.

Kessler D, Leibrecht I, Knappe J.

Institut für Biologische Chemie, Universität Heidelberg, Germany.

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.

PMID: 2015910 [PubMed - indexed for MEDLINE]

Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli.
J Biol Chem. 1992 Sep 5; 267(25):18073-9.

[J Biol Chem. 1992]
Molecular characteristics and transcription of the gene encoding a multifunctional alcohol dehydrogenase in relation to the deactivation of pyruvate formate-lyase in the ruminal bacterium Streptococcus bovis.
Arch Microbiol. 2004 Feb; 181(2):122-8. Epub 2003 Dec 16.

[Arch Microbiol. 2004]
Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins.
J Biol Chem. 2000 Oct 27; 275(43):33869-75.

[J Biol Chem. 2000]
Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli.
Mol Biochem Parasitol. 1994 Apr; 64(2):253-60.

[Mol Biochem Parasitol. 1994]
ReviewA radical-chemical route to acetyl-CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli.
FEMS Microbiol Rev. 1990 Aug; 6(4):383-98.

[FEMS Microbiol Rev. 1990]
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