Investigation of pyrophosphate versus ATP substrate selection in the Entamoeba histolytica acetate kinase.

ABSTRACT: Acetate kinase (ACK; E.C. 2.7.2.1), which catalyzes the interconversion of acetate and acetyl phosphate, is nearly ubiquitous in bacteria but is present only in one genus of archaea and certain eukaryotic microbes. All ACKs utilize ATP/ADP as the phosphoryl donor/acceptor in the respective directions of the reaction (acetate + ATP [Formula: see text] acetyl phosphate + ADP), with the exception of the Entamoeba histolytica ACK (EhACK) which uses pyrophosphate (PP_i)/inorganic phosphate (P_i) (acetyl phosphate + P_i  [Formula: see text] acetate + PP_i). Structural analysis and modeling of EhACK indicated steric hindrance by active site residues constricts entry to the adenosine pocket as compared to ATP-utilizing Methanosarcina thermophila ACK (MtACK).

SUBMITTER: Dang T 

PROVIDER: S-EPMC5517563 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature