Unusual Phosphoenolpyruvate (PEP) Synthetase-Like Protein Crucial to Enhancement of Polyhydroxyalkanoate Accumulation in Haloferax mediterranei Revealed by Dissection of PEP-Pyruvate Interconversion Mechanism.

ABSTRACT: Phosphoenolpyruvate (PEP)/pyruvate interconversion is a major metabolic point in glycolysis and gluconeogenesis and is catalyzed by various sets of enzymes in different Archaea groups. In this study, we report the key enzymes that catalyze the anabolic and catabolic directions of the PEP/pyruvate interconversion in Haloferax mediterranei The in silico analysis showed the presence of a potassium-dependent pyruvate kinase (PYK_Hm [HFX_0773]) and two phosphoenol pyruvate synthetase (PPS) candidates (PPS_Hm [HFX_0782] and a PPS homolog protein named PPS-like [HFX_2676]) in this strain. Expression of the pyk_Hm gene and pps_Hm was induced by glycerol and pyruvate, respectively; whereas the pps-like gene was not in

SUBMITTER: Chen J 

PROVIDER: S-EPMC6752022 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature