Computer simulations of the catalytic mechanism of wild-type and mutant β-phosphoglucomutase-Reference-Cited by-同舟云学术

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

Published:2018 Issue:12 Volume:16 Page:2060-2073
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Barrozo Alexandre¹²³⁴⁵,Liao Qinghua¹²³⁴⁵^ORCID,Esguerra Mauricio¹²³⁴⁵^ORCID,Marloie Gaël¹²³⁴⁵,Florián Jan⁶⁷⁸⁹^ORCID,Williams Nicholas H.¹⁰¹¹¹²¹³^ORCID,Kamerlin Shina Caroline Lynn¹²³⁴⁵^ORCID

Affiliation:

1. Science for Life Laboratory

2. Department of Cell and Molecular Biology

3. Uppsala University

4. S-75124 Uppsala

5. Sweden

6. Department of Chemistry and Biochemistry

7. Loyola University Chicago

8. Chicago

9. USA

10. Department of Chemistry

11. Sheffield University

12. Sheffield

13. UK

Abstract

β-Phosphoglucomutase (β-PGM) has served as an important model system for understanding biological phosphoryl transfer.

Funder

Vetenskapsrådet

Knut och Alice Wallenbergs Stiftelse

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/OB/C8OB00312B

Reference74 articles.

1. The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction

2. Comment on "The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction"

3. Response to Comment on "The Pentacovalent Phosphorus Intermediate of a Phosphoryl Transfer Reaction"

4. High-Energy Intermediate or Stable Transition State Analogue: Theoretical Perspective of the Active Site and Mechanism of β-Phosphoglucomutase

5. Chemical Confirmation of a Pentavalent Phosphorane in Complex with β-Phosphoglucomutase

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