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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kessler D,Leibrecht I,Knappe J

doi

10.1016/0014-5793(91)80358-a

subject

Has Abstract

pub_date

1991-04-09 00:00:00

pages

59-63

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80358-A

journal_volume

281

pub_type

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