¹H, ¹⁵N and ¹³C backbone resonance assignments of the P146A variant of β-phosphoglucomutase from Lactococcus lactis in its substrate-free form.

ABSTRACT: β-Phosphoglucomutase (βPGM) is a magnesium-dependent phosphoryl transfer enzyme that catalyses the reversible isomerisation of β-glucose 1-phosphate and glucose 6-phosphate, via two phosphoryl transfer steps and a β-glucose 1,6-bisphosphate intermediate. Substrate-free βPGM is an essential component of the catalytic cycle and an understanding of its dynamics would present significant insights into βPGM functionality, and enzyme catalysed phosphoryl transfer in general. Previously, 30 residues around the active site of substrate-free βPGM_WT were identified as undergoing extensive millisecond dynamics and were unassignable. Here we report ¹H, ¹⁵N and ¹³C backbone resonance assignments of the P146A variant (βPGM_P146A) in its substrate-fre

SUBMITTER: Cruz-Navarrete FA 

PROVIDER: S-EPMC6713671 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature