Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase.

ABSTRACT: Metabolic regulation occurs through precise control of enzyme activity. Allomorphy is a post-translational fine control mechanism where the catalytic rate is governed by a conformational switch that shifts the enzyme population between forms with different activities. β-Phosphoglucomutase (βPGM) uses allomorphy in the catalysis of isomerisation of β-glucose 1-phosphate to glucose 6-phosphate via β-glucose 1,6-bisphosphate. Herein, we describe structural and biophysical approaches to reveal its allomorphic regulatory mechanism. Binding of the full allomorphic activator β-glucose 1,6-bisphosphate stimulates enzyme closure, progressing through NAC I and NAC III conformers. Prior to phosphoryl transfer, loops positioned on the cap and core domains are brought into close proximity, modulating t

SUBMITTER: Cruz-Navarrete FA 

PROVIDER: S-EPMC11283535 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature