@article{cdb6f4656b4e4dfa98c0f5d3292b9363,
title = "Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase",
author = "Alexandre Barrozo and Qinghua Liao and Mauricio Esguerra and Ga{\"e}l Marloie and Jan Flori{\'a}n and Williams, \{Nicholas H.\} and Kamerlin, \{Shina Caroline Lynn\} and Jan Florian",
note = "β-Phosphoglucomutase (β-PGM) has served as an important model system for understanding biological phosphoryl transfer. This enzyme catalyzes the isomerization of β-glucose-1-phosphate to β-glucose-6-phosphate in a two-step process proceeding via a bisphosphate intermediate. The conventionally accepted mechanism is that both steps are concerted processes involving acid-base catalysis from a nearby aspartate (D10) side chain.",
year = "2018",
month = jan,
day = "1",
doi = "10.1039/C8OB00312B",
language = "American English",
volume = "16",
journal = "Organic and Biomolecular Chemistry",
number = "12",
}