PYRUVATE-FORMATE-LYASE-DEACTIVASE AND ACETYL-COA REDUCTASE ACTIVITIES OF ESCHERICHIA-COLI RESIDE ON A POLYMERIC PROTEIN PARTICLE ENCODED BY ADHE

被引：127

作者：

KESSLER, D ^{[1
]}

LEIBRECHT, I ^{[1
]}

KNAPPE, J ^{[1
]}

机构：

[1] UNIV HEIDELBERG,INST BIOL CHEM,IM NEUENHEIMER FELD 501,W-6900 HEIDELBERG,GERMANY

来源：

FEBS LETTERS | 1991年 / 281卷 / 1-2期

关键词：

FE-2+-ACTIVATION; SPIROSOME; NUCLEOTIDE SEQUENCE; ANAEROBIC INDUCTION;

D O I：

10.1016/0014-5793(91)80358-A

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：59 / 63

页数：5

共 16 条

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