STUDIES ON A MUTANT FORM OF ESCHERICHIA-COLI CITRATE SYNTHASE DESENSITIZED TO ALLOSTERIC EFFECTORS

被引:23
作者
DANSON, MJ [1 ]
HARFORD, S [1 ]
WEITZMAN, PDJ [1 ]
机构
[1] UNIV BATH, SCH BIOL SCI, DEPT BIOCHEM, BATH BA2 7AY, SOMERSETSHIRE, ENGLAND
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1979年 / 101卷 / 02期
关键词
D O I
10.1111/j.1432-1033.1979.tb19746.x
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
Naturally-occurring citrate synthases fall into distinct molecular and catalytic types. Gram-negative bacteria produce a large enzyme, allosterically inhibited by NADH and, in the facultative anaerobes such as E. coli, also by 2-oxoglutarate. Gram-positive bacteria and all eukaryotes produce a small citrate synthase which is insensitive to these metabolites. As a complement to structure-function studies, the possibility of genetically altering one type of citrate synthase to the other was explored. By mutagenesis and suitable selection, a mutant of E. coli whose citrate synthase is both small and insensitive to NADH and 2-oxoglutarate was isolated. Some characteristics of the enzyme are described. Such mutant enzymes offer a novel approach to the study of citrate synthase, its regulation and its natural diversity.
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页码:515 / 521
页数:7
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