Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase

Alexandre Barrozo; Qinghua Liao; Mauricio Esguerra; Gaël Marloie; Jan Florián; Nicholas H. Williams; Shina Caroline Lynn Kamerlin; Jan Florian

doi:10.1039/C8OB00312B

Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase

Alexandre Barrozo
, Qinghua Liao
, Mauricio Esguerra
, Gaël Marloie
, Jan Florián
, Nicholas H. Williams
, Shina Caroline Lynn Kamerlin
, Jan Florian

Science for Life Laboratory
Loyola University Chicago
University of Sheffield

Research output: Contribution to journal › Article › peer-review

Original language	American English
Journal	Organic and Biomolecular Chemistry
Volume	16
Issue number	12
DOIs	https://doi.org/10.1039/C8OB00312B
State	Published - Jan 1 2018

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Chemistry

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@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",

}

TY - JOUR

T1 - Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase

AU - Barrozo, Alexandre

AU - Liao, Qinghua

AU - Esguerra, Mauricio

AU - Marloie, Gaël

AU - Florián, Jan

AU - Williams, Nicholas H.

AU - Kamerlin, Shina Caroline Lynn

AU - Florian, Jan

N1 - 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.

PY - 2018/1/1

Y1 - 2018/1/1

UR - http://eprints.whiterose.ac.uk/128815/

U2 - 10.1039/C8OB00312B

DO - 10.1039/C8OB00312B

M3 - Article

VL - 16

JO - Organic and Biomolecular Chemistry

JF - Organic and Biomolecular Chemistry

IS - 12

ER -

Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase

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