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Pyruvate‐formate‐lyase‐deactivase and acetyl‐CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE
Author(s) -
Kessler Dorothea,
Leibrecht Iris,
Knappe Joachim
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80358-a
Subject(s) - escherichia coli , biochemistry , mutant , gene , chemistry , formate , reductase , acetaldehyde , dna , enzyme , biology , ethanol , catalysis
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 anaecrobic 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 (∼ 40 × 96 kDa) requiring Fe 2+ for all functions.