Department of Biochemistry and Molecular Biology, James Cook University, Townsville, Queensland 4811, Australia.
BMC Biochem. 2010 Jan 3;11:1. doi: 10.1186/1471-2091-11-1.
Phosphoenolpyruvate synthetase (PEPS; EC 2.7.9.2) catalyzes the synthesis of phosphoenolpyruvate from pyruvate in Escherichia coli when cells are grown on a three carbon source. It also catalyses the anabolic conversion of pyruvate to phosphoenolpyruvate in gluconeogenesis. A bioinformatics search conducted following the successful cloning and expression of maize leaf pyruvate, orthophosphate dikinase regulatory protein (PDRP) revealed the presence of PDRP homologs in more than 300 bacterial species; the PDRP homolog was identified as DUF299.
This paper describes the cloning and expression of both PEPS and DUF299 from E. coli and establishes that E. coli DUF299 catalyzes both the ADP-dependent inactivation and the Pi-dependent activation of PEPS.
This paper represents the first report of a bifunctional regulatory enzyme catalysing an ADP-dependent phosphorylation and a Pi-dependent pyrophosphorylation reaction in bacteria.
当大肠杆菌在三碳源上生长时，磷酸烯醇丙酮酸合成酶（PEPS；EC 2.7.9.2）催化从丙酮酸合成磷酸烯醇丙酮酸。它还催化糖异生中丙酮酸到磷酸烯醇丙酮酸的合成代谢转化。在成功克隆和表达玉米叶丙酮酸、 orthophosphate dikinase 调节蛋白（PDRP）后进行的生物信息学搜索表明，超过 300 种细菌中存在 PDRP 同源物；PDRP 同源物被鉴定为 DUF299。
本文描述了大肠杆菌中 PEPS 和 DUF299 的克隆和表达，并证实大肠杆菌 DUF299 催化 PEPS 的 ADP 依赖性失活和 Pi 依赖性激活。
本文首次报道了细菌中一种双功能调节酶催化 ADP 依赖性磷酸化和 Pi 依赖性焦磷酸化反应。
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