| Literature DB >> 31621997 |
Ryan R Hughes1, Khaled A Shaaban1, Larissa V Ponomareva1, Jamie Horn1, Chunhui Zhang1, Chang-Guo Zhan1, S Randal Voss2, Markos Leggas1, Jon S Thorson1.
Abstract
Herein we describe the ability of the permissive glycosyltransferase (GT) OleD Loki to convert a diverse set of >15 histone deacetylase (HDAC) inhibitors (HDACis) into their corresponding hydroxamate glycosyl esters. Representative glycosyl esters were subsequently evaluated in assays for cancer cell line cytotoxicity, chemical and enzymatic stability, and axolotl embryo tail regeneration. Computational substrate docking models were predictive of enzyme-catalyzed turnover and suggest certain HDACis may form unproductive, potentially inhibitory, complexes with GTs.Entities:
Keywords: HDAC; glucosylation; glycosyltransferase; histone deacetylase
Mesh:
Substances:
Year: 2019 PMID: 31621997 PMCID: PMC7124993 DOI: 10.1002/cbic.201900601
Source DB: PubMed Journal: Chembiochem ISSN: 1439-4227 Impact factor: 3.164