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Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.

Lloyd, Matthew D, Yevglevskis, Maksims, Nathubhai, Amit, James, Tony D, Threadgill, Michael D and Woodman, Timothy J (2021) Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition. Chemical Society reviews, 50 (10). pp. 5952-5984. ISSN 1460-4744

Item Type: Article


Racemases and epimerases catalyse changes in the stereochemical configurations of chiral centres and are of interest as model enzymes and as biotechnological tools. They also occupy pivotal positions within metabolic pathways and, hence, many of them are important drug targets. This review summarises the catalytic mechanisms of PLP-dependent, enolase family and cofactor-independent racemases and epimerases operating by a deprotonation/reprotonation (1,1-proton transfer) mechanism and methods for measuring their catalytic activity. Strategies for inhibiting these enzymes are reviewed, as are specific examples of inhibitors. Rational design of inhibitors based on substrates has been extensively explored but there is considerable scope for development of transition-state mimics and covalent inhibitors and for the identification of inhibitors by high-throughput, fragment and virtual screening approaches. The increasing availability of enzyme structures obtained using X-ray crystallography will facilitate development of inhibitors by rational design and fragment screening, whilst protein models will facilitate development of transition-state mimics.

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Item ID: 13574
Identification Number:
ISSN: 1460-4744
Official URL:

Users with ORCIDS

ORCID for Matthew D Lloyd: ORCID iD
ORCID for Amit Nathubhai: ORCID iD
ORCID for Tony D James: ORCID iD

Catalogue record

Date Deposited: 22 Jun 2021 13:47
Last Modified: 22 Jun 2021 14:00


Author: Matthew D Lloyd ORCID iD
Author: Amit Nathubhai ORCID iD
Author: Tony D James ORCID iD
Author: Maksims Yevglevskis
Author: Michael D Threadgill
Author: Timothy J Woodman

University Divisions

Faculty of Health Sciences and Wellbeing > School of Pharmacy and Pharmaceutical Sciences

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