Chemical and Biochemical Strategies To Explore the Substrate Recognition of O-GlcNAc-Cycling Enzymes.
O-GlcNAc
chemical probes
glycosylation
microarrays
substrate recognition
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
01 02 2019
01 02 2019
Historique:
received:
19
08
2018
pubmed:
11
9
2018
medline:
28
11
2019
entrez:
11
9
2018
Statut:
ppublish
Résumé
The O-linked N-acetylglucosamine (O-GlcNAc) modification is an essential component in cell regulation. A single pair of human enzymes conducts this modification dynamically on a broad variety of proteins: O-GlcNAc transferase (OGT) adds the GlcNAc residue and O-GlcNAcase (OGA) hydrolyzes it. This modification is dysregulated in many diseases, but its exact effect on particular substrates remains unclear. In addition, no apparent sequence motif has been found in the modified proteins, and the factors controlling the substrate specificity of OGT and OGA are largely unknown. In this minireview, we will discuss recent developments in chemical and biochemical methods toward addressing the challenge of OGT and OGA substrate recognition. We hope that the new concepts and knowledge from these studies will promote research in this area to advance understanding of O-GlcNAc regulation in health and disease.
Identifiants
pubmed: 30199580
doi: 10.1002/cbic.201800481
pmc: PMC6433133
mid: NIHMS1018170
doi:
Substances chimiques
N-Acetylglucosaminyltransferases
EC 2.4.1.-
O-GlcNAc transferase
EC 2.4.1.-
hexosaminidase C
EC 3.2.1.50
beta-N-Acetylhexosaminidases
EC 3.2.1.52
Acetylglucosamine
V956696549
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
312-318Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM121718
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM126300
Pays : United States
Informations de copyright
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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