Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms.
Journal
Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
received:
23
08
2018
accepted:
05
12
2018
pubmed:
2
2
2019
medline:
9
6
2020
entrez:
2
2
2019
Statut:
ppublish
Résumé
Dysregulation of nuclear and cytoplasmic O-linked β-N-acetylglucosamine (O-GlcNAc) cycling is implicated in a range of diseases including diabetes and cancer. This modification maintains cellular homeostasis by regulating several biological processes, such as cell signaling. This highly regulated cycle is governed by two sole essential enzymes, O-GlcNAc transferase and O-GlcNAcase that add O-GlcNAc and remove it from over a thousand substrates, respectively. Until recently, due to lack of structural information, the mechanism of substrate recognition has eluted researchers. Here, we review recent successes in structural characterization of these enzymes and how this information has illuminated key features essential for catalysis and substrate recognition. Additionally, we highlight recent studies which have used this information to expand our understanding of substrate specificity by each enzyme.
Identifiants
pubmed: 30708324
pii: S0959-440X(18)30099-X
doi: 10.1016/j.sbi.2018.12.003
pmc: PMC6656603
mid: NIHMS1516959
pii:
doi:
Substances chimiques
Transferases
EC 2.-
Acetylglucosamine
V956696549
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
97-106Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM094263
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM121718
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM126300
Pays : United States
Informations de copyright
Copyright © 2018 Elsevier Ltd. All rights reserved.
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