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Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli.
FEMS Microbiol Lett. 1998 Sep 15; 166(2):333-9.FM

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.

Authors+Show Affiliations

Department of Biological Sciences, Napier University, Edinburgh, UK. m.el-mansi@napier.ac.uk

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9770290

Citation

el-Mansi, E M.. "Control of Metabolic Interconversion of Isocitrate Dehydrogenase Between the Catalytically Active and Inactive Forms in Escherichia Coli." FEMS Microbiology Letters, vol. 166, no. 2, 1998, pp. 333-9.
el-Mansi EM. Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli. FEMS Microbiol Lett. 1998;166(2):333-9.
el-Mansi, E. M. (1998). Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli. FEMS Microbiology Letters, 166(2), 333-9.
el-Mansi EM. Control of Metabolic Interconversion of Isocitrate Dehydrogenase Between the Catalytically Active and Inactive Forms in Escherichia Coli. FEMS Microbiol Lett. 1998 Sep 15;166(2):333-9. PubMed PMID: 9770290.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Control of metabolic interconversion of isocitrate dehydrogenase between the catalytically active and inactive forms in Escherichia coli. A1 - el-Mansi,E M, PY - 1998/10/14/pubmed PY - 1998/10/14/medline PY - 1998/10/14/entrez SP - 333 EP - 9 JF - FEMS microbiology letters JO - FEMS Microbiol Lett VL - 166 IS - 2 N2 - 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. SN - 0378-1097 UR - https://www.unboundmedicine.com/medline/citation/9770290/Control_of_metabolic_interconversion_of_isocitrate_dehydrogenase_between_the_catalytically_active_and_inactive_forms_in_Escherichia_coli_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1111/j.1574-6968.1998.tb13909.x DB - PRIME DP - Unbound Medicine ER -