Trapping and retaining intermediates in glycosyltransferases
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 SNi mechanism. In a recent article in th...
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| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2023 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/341637 |
| Acceso en línea: | http://hdl.handle.net/10261/341637 |
| Access Level: | acceso abierto |
| Palabra clave: | Escherichia coli Cell surface Capsular polysaccharide Glycolipid biosynthesis Glycosyltransferase CAZyme Enzyme structure Enzyme mechanism Enzyme catalysis |
| Sumario: | 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 SNi 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. |
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