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
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
收藏
页码:59 / 63
页数:5
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