Tolentino, Rebecca, Chastain, Chris, and Burnell, Jim (2013) Identification of the amino acid involved in the regulation of bacterial pyruvate, orthophosphate dikinase and phosphoenolpyruvate synthetase. Advances in Biological Chemistry, 3 (3A). pp. 12-21.

Preview

PDF (Published Version) - Published Version Available under License Creative Commons Attribution. Download (355kB)

Abstract

phosphoenolpyruvate synthetase (PEPS) catalyze the conversion of pyruvate to phosphoenolpyruvate (PEP). Both are regulated by a phosphorylation-dephosphorylation mechanism involving a bifunctional serine/threonine kinase and a pyrophosphorylase (PPDK regulatory protein, PDRP, and PEPS regulatory protein, PSRP, respectively). In plants the regulatory mechanism involves phosphorylation of a threonine residue that is separated by a single amino acid from the histidine residue that forms a phosphorylated intermediate during catalysis. Using antibodies, we demonstrated that the regulation of both Listeria monocytogenes PPDK and Escherichia coli PEP synthetase involves the phosphorylation of a threonine residue located close to the catalytic histidine residue. The amino acid located between the regulatory threonine and the catalytic histidine is highly conserved being serine in PPDK and cysteine in PEPS. Using site-directed mutagenesis we have shown that both PPDK and PEPS in which the serine and cysteine residues, respectively, were substituted with an alanine the enzymes could be regulated indicating that the serine and cysteine residues, respectively, are not essential for regulation. We also demonstrated that altering the intermediate amino acid did not alter the specificity of the regulatory proteins for their protein substrates.

Item ID:	27130
Item Type:	Article (Research - C1)
ISSN:	2162-2191
Keywords:	Escherichia coli, Listeria monocytogenes, enzyme regulation, phosphorylation/dephosphorylation, pyruvate orthophosphate dikinase, PEP synthetase
Related URLs:	http://www.scirp.org/journal/abc/
Additional Information:	This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Date Deposited:	26 Jun 2013 22:46
FoR Codes:	06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060104 Cell Metabolism @ 100%
SEO Codes:	97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
Downloads:	Total: 349 Last 12 Months: 7
	More Statistics