Structural comparisons of phosphoenolpyruvate carboxykinases reveal the evolutionary trajectories of these phosphodiester energy conversion enzymes.

ABSTRACT: Inorganic pyrophosphate (PP_i) consists of two phosphate molecules and can act as an energy and phosphate donor in cellular reactions, similar to ATP. Several kinases use PP_i as a substrate, and these kinases have recently been suggested to have evolved from ATP-dependent functional homologs, which have significant amino acid sequence similarity to PP_i-utilizing enzymes. In contrast, phosphoenolpyruvate carboxykinase (PEPCK) can be divided into three types according to the phosphate donor (ATP, GTP, or PPi), and the amino acid sequence similarity of these PEPCKs is too low to confirm that they share a common ancestor. Here we solved the crystal structure of a PP_i-PEPCK homolog from the bacterium Actinomyces israelii at 2.6 Å resolution and

SUBMITTER: Chiba Y 

PROVIDER: S-EPMC6916476 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature