Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE.
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.
Kessler
D
D
Institut für Biologische Chemie, Universität Heidelberg, Germany.
Leibrecht
I
I
Knappe
J
J
D000426:Alcohol Dehydrogenase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D000693:Anaerobiosis; D001483:Base Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics* / Q000254:growth & development; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D007700:Kinetics; D008969:Molecular Sequence Data; D009097:Multienzyme Complexes / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010957:Plasmids; D015183:Restriction Mapping
D029968:Escherichia coli Proteins; D009097:Multienzyme Complexes; D000426:Alcohol Dehydrogenase; C068383:adhE protein, E coli; D000445:Aldehyde Oxidoreductases; C027014:acetaldehyde dehydrogenase (acylating)