Rational design of a cyclohexanone dehydrogenase for enhanced α,β-desaturation and substrate specificity-Reference-Cited by-同舟云学术

Rational design of a cyclohexanone dehydrogenase for enhanced α,β-desaturation and substrate specificity

Published:2024 Issue:13 Volume:15 Page:4969-4980
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Singh Warispreet¹,Brown Nicola L.¹,McCue Hannah V.²,Marriott Sophie R.³,Wilson Richard C.³,Perry Justin¹^ORCID,Turkenburg Johan P.⁴,Dubey Kshatresh D.⁵,Prior Stephen H.⁶,Carnell Andrew J.⁷,Taylor Edward J.³,Black Gary W.¹^ORCID

Affiliation:

1. Hub for Biotechnology in Build Environment, Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne, NE1 8ST, UK

2. Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Crown Street, Liverpool, L69 7ZB, UK

3. Department of Life Sciences, University of Lincoln, Lincoln, LN6 7TS, UK

4. Structural Biology Laboratory, Department of Chemistry, University of York, YO10 5DD, UK

5. Department of Chemistry, Center for Informatics, School of Natural Sciences, Shiv Nadar University, Uttar Pradesh-201314, India

6. School of Chemistry, University of Lincoln, Lincoln LN6 7DL, UK

7. Department of Chemistry, University of Liverpool, Crown Street, Liverpool, L69 7ZD, UK

Abstract

The W113A cyclohexanone dehydrogenase variant had improved substrate scope, i.e., accepting a bulkier compound, compared to wildtype enzyme. Structural analysis of the variant revealed a broader, more open active site, explaining the new substrate scope.

Funder

Biotechnology and Biological Sciences Research Council

Department of Biotechnology, Ministry of Science and Technology, India

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/SC/D3SC04009G

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