Conserved Active Site Architecture Between Bacterial Cellulose and Chitin Synthases.

Autor: Shamshoum M; Department of Plant and Environmental Sciences, Weizmann Institute of Science, 234 Herzl St., Rehovot, 7610001, Israel., Natalio F; Department of Plant and Environmental Sciences, Weizmann Institute of Science, 234 Herzl St., Rehovot, 7610001, Israel.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2023 Aug 15; Vol. 24 (16), pp. e202300388. Date of Electronic Publication: 2023 Jun 12.
DOI: 10.1002/cbic.202300388
Abstrakt: Glycosyltransferases (GTs) are a large and diverse group of enzymes responsible for catalyzing the formation of a glycosidic bond between a donor molecule, usually a monosaccharide, and a wide range of acceptor molecules, thus, playing critical roles in various essential biological processes. Chitin and cellulose synthases are two inverting processive integral membrane GTs, belonging to the type-2 family involved in the biosynthesis of chitin and cellulose, respectively. Herein, we report that bacterial cellulose and chitin synthases share an E-D-D-ED-QRW-TK active site common motif that is spatially co-localized. This motif is conserved among distant bacterial evolutionary species despite their low amino acid sequence and structural similarities between them. This theoretical framework offers a new perspective to the current view that bacterial cellulose and chitin synthases are substrate specific and that chitin and cellulose are organism specific. It lays the ground for future in vivo and in silico experimental assessment of cellulose synthase catalytic promiscuity against uridine diphosphate N-acetylglucosamine and chitin synthase against uridine diphosphate glucose, respectively.
(© 2023 The Authors. ChemBioChem published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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