The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β-Phosphoglucomutase-Reference-Cited by-同舟云学术

The Relationship between Enzyme Conformational Change, Proton Transfer, and Phosphoryl Transfer in β-Phosphoglucomutase

Published:2021-10-07 Issue:21 Volume:11 Page:12840-12849
ISSN:2155-5435
Container-title:ACS Catalysis
language:en
Short-container-title:ACS Catal.

Author:

Robertson Angus J.¹,Wilson Alex L.²,Burn Matthew J.²,Cliff Matthew J.²,Popelier Paul L. A.²,Waltho Jonathan P.¹²^ORCID

Affiliation:

1. Department of Molecular Biology and Biotechnology, Krebs Institute for Biomolecular Research, The University of Sheffield, Sheffield S10 2TN, United Kingdom

2. Department of Chemistry, Manchester Institute of Biotechnology, The University of Manchester, Manchester M1 7DN, United Kingdom

Funder

Engineering and Physical Sciences Research Council

Biotechnology and Biological Sciences Research Council

Publisher

American Chemical Society (ACS)

Subject

Catalysis,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acscatal.1c01389

Reference40 articles.

1. Enzyme-Catalyzed Phosphoryl Transfer Reactions

2. The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases

3. Enzymatic Mechanisms of Phosphate and Sulfate Transfer

4. Biological Phosphoryl-Transfer Reactions: Understanding Mechanism and Catalysis

5. Near attack conformers dominate -phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate

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