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

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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 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 Fe2+ for all functions. © 1991.

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Kessler, D., Leibrecht, I., & 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 Letters, 281(1–2), 59–63. https://doi.org/10.1016/0014-5793(91)80358-A

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