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Current Topics in Biochemical Research   Volumes    Volume 13  Issue 2
Abstract
A fourth level of regulation of PEP synthetase in Escherichia coli; implications of ADP-dependent inactivation
Rebecca Tolentino, Jim Burnell
Pages: 27 - 38
Number of pages: 12
Current Topics in Biochemical Research
Volume 13  Issue 2

Copyright © 2011 Research Trends. All rights reserved

ABSTRACT
 
In Escherichia coli, phosphoenolpyruvate synthetase (PEPS) catalyzes the conversion of pyruvate to phosphoenolpyruvate (PEP). The enzyme is regulated at four levels: it is regulated at the level of transcription by the carbon source available for growth, by regulation of mRNA stability, by metabolic intermediates, and, by a recently discovered phosphorylation/ dephosphorylation mechanism. This manuscript reviews our current understanding of the four levels of regulation of the peps gene and its gene product and reports on recent advances made in our understanding of the post-translational regulation of the protein. A model is proposed that summarizes the control of pyruvate metabolism in E. coli (and other bacterial species possessing PEP synthetase or pyruvate, orthophosphate dikinase); whether pyruvate is used for the generation of ATP or whether pyruvate is converted to PEP for use in gluconeogenesis, aromatic amino acid synthesis and other anabolic pathways. Finally, we provide some suggestions regarding the use of PEPS in the biotechnology industry based on our understanding of the regulation of the enzyme.
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