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PMID: 2015910 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 281 ·No. 1-2 ·1991-04-09 ·Pages 59-63

Kessler D, Leibrecht I, Knappe J

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.

Related Genes
MeSH Terms
Alcohol Dehydrogenase/genetics,isolation & purification,metabolism Aldehyde Oxidoreductases/genetics,isolation & purification,metabolism Anaerobiosis Base Sequence Escherichia coli/enzymology,genetics,growth & development Escherichia coli Proteins Genes, Bacterial Kinetics Molecular Sequence Data Multienzyme Complexes/genetics,isolation & purification,metabolism Plasmids Restriction Mapping
Chemicals
Escherichia coli Proteins Multienzyme Complexes Alcohol Dehydrogenase adhE protein, E coli Aldehyde Oxidoreductases acetaldehyde dehydrogenase (acylating)
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kessler D
Institut für Biologische Chemie, Universität Heidelberg, Germany.
Leibrecht I
Knappe J
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1991-04-09
Pages
59-63
Language
English
Region
England
NLM ID
0155157
Subset
IM
Databases
GENBANK
X58797, X58798, X58799, X58800, X58801, X58802, X58803, X59501, X59502, X62841
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