Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli.

Abstract:

:The enzymic interconversion of Escherichia coli isocitrate dehydrogenase (ICDH) between the catalytically active and inactive forms is mediated through the activities of ICDH-kinase/phosphatase in response to changes in the metabolic environment. In this study, the use of mutant strains devoid of isocitrate lyase (aceA:: Tn10) and pyruvate dehydrogenase activities revealed that the signal which triggers the reversible inactivation of ICDH in vivo is not directly related to acetate itself, but rather to the need to maintain high intracellular levels of isocitrate and free co-enzyme A. The use of these mutants also revealed, rather unexpectedly, that acetate grown cells contain more ICDH protein than those grown with other carbon sources and that the catalytic activity of ICDH kinase/phosphatase is in excess of cellular demands. Furthermore, this study also revealed the presence of a 50-kDa (+/- 2 kDa) acetate-specific polypeptide, the identity of which has yet to be established.

journal_name

FEMS Microbiol Lett

authors

el-Mansi EM

doi

10.1111/j.1574-6968.1998.tb13909.x

subject

Has Abstract

pub_date

1998-09-15 00:00:00

pages

333-9

issue

2

eissn

0378-1097

issn

1574-6968

pii

S0378109798003516

journal_volume

166

pub_type

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