Disease relevance of pps

• The pps gene was cloned by an in vivo cloning method using a mini-Mulac bacteriophage containing a plasmid replicon [1].
• We have cloned the pps gene, coding for PEP synthase, of Escherichia coli [1].
• Characterization of phosphoenolpyruvate synthase mutants in Salmonella typhimurium [2].
• The enteric bacteria are able to grow by utilizing three-carbon compounds (pyruvate, lactate, and alanine) as sole carbon sources only if they have a functional phosphoenolpyruvate synthase (PEP synthase) [2].

High impact information on pps

• In vivo, neither the operators of the fru operon nor of the pps operon, the natural targets for FruR, were recognized, but the scr operators were [3].
• Instead, the phosphotransferase system appeared to regulate gluconeogenesis by controlling the activities of phosphoenolpyruvate carboxykinase and phosphoenolpyruvate synthase [4].
• By using bacteriophage P22, the pps mutations isolated in this study were found to be contransducible with genetic markers in both the aroD and btuC genes [2].
• The position of the pps gene of the plasmid was localized by restriction analysis of isolated transposon insertions and the determination of the PEP synthase activities of the different clones [1].
• Measurements of the galactokinase activity showed that the absence of the Fructose PTS proteins has no significant influence on the regulation of the pps gene [1].

Biological context of pps

• PEP synthase catalyzes the phosphorylation of pyruvate to PEP with the hydrolysis of ATP to AMP [2].

Associations of pps with chemical compounds

• The pps gene is also under catabolite repression, but the addition of adenosine 3',5'-cyclic monophosphate (cyclic AMP) to cells grown in the presence of glucose does not relieve this repression [2].
• The ATP-catalyzed reaction is dependent on phosphoenolpyruvate synthase, however, and is due to prior conversion of ATP to phosphoenolpyruvate [5].

References