OleD Loki as a Catalyst for Hydroxamate Glycosylation

Ryan R. Hughes, Khaled A. Shaaban, Larissa V. Ponomareva, Jamie Horn, Chunhui Zhang, Chang Guo Zhan, S. Randal Voss, Markos Leggas, Jon S. Thorson

Research output: Contribution to journalArticlepeer-review

6 Scopus citations

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.

Original languageEnglish
Pages (from-to)952-957
Number of pages6
JournalChemBioChem
Volume21
Issue number7
DOIs
StatePublished - Apr 1 2020

Bibliographical note

Publisher Copyright:
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim

Keywords

  • HDAC
  • glucosylation
  • glycosyltransferase
  • histone deacetylase

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Fingerprint

Dive into the research topics of 'OleD Loki as a Catalyst for Hydroxamate Glycosylation'. Together they form a unique fingerprint.

Cite this