Regulation of the pyrimidine biosynthetic pathway by lysine acetylation of E. coli OPRTase.

ABSTRACT: The de novo pyrimidine biosynthesis pathway is an important route due to the relevance of its products, its implications in health and its conservation among organisms. Here, we investigated the regulation by lysine acetylation of this pathway. To this aim, intracellular and extracellular metabolites of the route were quantified, revealing a possible blockage of the pathway by acetylation of the OPRTase enzyme (orotate phosphoribosyltransferase). Chemical acetylation of OPRTase by acetyl-P involved a decrease in enzymatic activity. To test the effect of acetylation in this enzyme, K26 and K103 residues were selected to generate site-specific acetylated proteins. Several differences were observed in kinetic parameters, emphasizing that the k_cat of these mutants showed a strong de

SUBMITTER: Lozano-Terol G 

PROVIDER: S-EPMC10087573 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature