Asymmetric Ene-Reduction by F420-Dependent Oxidoreductases B (FDOR-B) from Mycobacterium smegmatis

Authors
Kang, Suk WooAntoney, JamesLupton, David W.Speight, RobertScott, ColinJackson, Colin J.
Issue Date
2023-04
Publisher
John Wiley & Sons Ltd.
Citation
ChemBioChem, v.24, no.8
Abstract
Asymmetric reduction by ene-reductases has received considerable attention in recent decades. While several enzyme families possess ene-reductase activity, the Old Yellow Enzyme (OYE) family has received the most scientific and industrial attention. However, there is a limited substrate range and few stereocomplementary pairs of current ene-reductases, necessitating the development of a complementary class. Flavin/deazaflavin oxidoreductases (FDORs) that use the uncommon cofactor F-420 have recently gained attention as ene-reductases for use in biocatalysis due to their stereocomplementarity with OYEs. Although the enzymes of the FDOR-As sub-group have been characterized in this context and reported to catalyse ene-reductions enantioselectively, enzymes from the similarly large, but more diverse, FDOR-B sub-group have not been investigated in this context. In this study, we investigated the activity of eight FDOR-B enzymes distributed across this sub-group, evaluating their specific activity, kinetic properties, and stereoselectivity against alpha,beta-unsaturated compounds. The stereochemical outcomes of the FDOR-Bs are compared with enzymes of the FDOR-A sub-group and OYE family. Computational modelling and induced-fit docking are used to rationalize the observed catalytic behaviour and proposed a catalytic mechanism.
Keywords
F420H2-DEPENDENT REDUCTASES; COFACTOR; COENZYME; FAMILY; F-420; GLUCOSE-6-PHOSPHATE-DEHYDROGENASE; IDENTIFICATION; COVERAGE; ENZYMES; biocatalysis; deazaflavin; F-420; ene-reductases; Mycobacterium smegmatis
ISSN
1439-4227
URI
https://pubs.kist.re.kr/handle/201004/113871
DOI
10.1002/cbic.202200797
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KIST Article > 2023
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