Trapping and retaining intermediates in glycosyltransferases

Marcelo E Guerin

doi:10.1016/j.jbc.2023.105006

Trapping and retaining intermediates in glycosyltransferases

J Biol Chem. 2023 Aug;299(8):105006. doi: 10.1016/j.jbc.2023.105006. Epub 2023 Jul 1.

Author

Marcelo E Guerin¹

Affiliation

¹ Department of Structural and Molecular Biology, Structural Glycobiology Laboratory, Molecular Biology Institute of Barcelona (IBMB), Spanish National Research Council (CSIC), Barcelona, Catalonia, Spain. Electronic address: mrccri@ibmb.csic.es.

Abstract

Glycosyltransferases (GTs) attach sugar molecules to a broad range of acceptors, generating a remarkable amount of structural diversity in biological systems. GTs are classified as either "retaining" or "inverting" enzymes. Most retaining GTs typically use an S_Ni mechanism. In a recent article in the JBC, Doyle et al. demonstrate a covalent intermediate in the dual-module KpsC GT (GT107) supporting a double displacement mechanism.

Keywords: CAZyme; Escherichia coli; capsular polysaccharide; cell surface; enzyme catalysis; enzyme mechanism; enzyme structure; glycolipid biosynthesis; glycosyltransferase.

Publication types

Editorial
Comment

MeSH terms

Glycosyltransferases* / chemistry

Substances

Glycosyltransferases