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大肠杆菌的丙酮酸-甲酸裂解酶失活酶和乙酰辅酶A还原酶活性存在于由adhE编码的聚合蛋白颗粒上。

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

作者信息

Kessler D, Leibrecht I, Knappe J

机构信息

Institut für Biologische Chemie, Universität Heidelberg, Germany.

出版信息

FEBS Lett. 1991 Apr 9;281(1-2):59-63. doi: 10.1016/0014-5793(91)80358-a.

DOI:10.1016/0014-5793(91)80358-a
PMID:2015910
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.

摘要

克隆并测序了一个4.8 kb的DNA片段，该片段包含PFL去激活酶的结构基因（2.7 kb）以及2 kb的5'侧翼区域，其中含有厌氧诱导元件。一个缺乏去激活酶的突变体被证明在以葡萄糖进行厌氧生长时需要外源电子受体。这揭示了PFL去激活酶与大肠杆菌的乙醇脱氢酶和乙醛脱氢酶的同一性。这种多酶代表一种同聚蛋白（约40×96 kDa），其所有功能都需要Fe2+。

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