Details:

Alternative Title:
Chembiochem
Personal Author:
Hughes, Ryan R. ; Shaaban, Khaled A. ; Ponomareva, Larissa V. ; Horn, Jamie ; Zhang, Chunhui ; ... More +
Hughes, Ryan R. ; Shaaban, Khaled A. ; Ponomareva, Larissa V. ; Horn, Jamie ; Zhang, Chunhui ; Zhan, Chang-Guo ; Voss, S. Randal ; Leggas, Markos ; Thorson, Jon S. Less -
Description:
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.
Subjects:
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Article Glucosylation Glycosyltransferase HDAC Histone Deacetylase
Source:
Chembiochem. 21(7):952-957
Pubmed ID:
31621997
Pubmed Central ID:
PMC7124993
Document Type:
Journal Article
Funding:
R37 AI52218/GM/NIGMS NIH HHS/United States ; R24 OD21479/CD/ODCDC CDC HHS/United States ; UL1 TR000117/TR/NCATS NIH HHS/United States ; UL1 TR001998/TR/NCATS NIH HHS/United States ; R37 AI052218/AI/NIAID NIH HHS/United States ; ... More +
R37 AI52218/GM/NIGMS NIH HHS/United States ; R24 OD21479/CD/ODCDC CDC HHS/United States ; UL1 TR000117/TR/NCATS NIH HHS/United States ; UL1 TR001998/TR/NCATS NIH HHS/United States ; R37 AI052218/AI/NIAID NIH HHS/United States ; R24 OD021479/OD/NIH HHS/United States Less -
Collection(s):
CDC Public Access
Main Document Checksum:
[+]
urn:sha256:50e42447d649736b0ca01db8692bc9764aab6afa7c5d12bf15313030bf9b27d0
Download URL:
https://stacks.cdc.gov/view/cdc/86403/cdc_86403_DS1.pdf
File Type:

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