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Article Dans Une Revue Biochemical Society Transactions Année : 2017

OGT: a short overview of an enzyme standing out from usual glycosyltransferases

Résumé

O-GlcNAcylation is a highly dynamic post-translational modification whose level depends on nutrient status. Only two enzymes regulate O-GlcNAcylation cycling, the glycosyltransferase OGT (O-GlcNAc transferase) and the glycoside hydrolase OGA (O-GlcNAcase), that add and remove the GlcNAc moiety to and from acceptor proteins, respectively. During the last 30 years, OGT has emerged as a master regulator of cell life with O-GlcNAcylation being found in viruses, bacteria, insects, protists and metazoans. The study of OGT in different biological systems opens new perspectives for understanding this enzyme in many kingdoms of life. In this review, we summarize recent and older findings regarding the distribution of OGT in living organisms.
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hal-03167805 , version 1 (12-03-2021)

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Moyira Osny Aquino-Gil, Annick Pierce, Yobana Perez-Cervera, Edgar Zenteno, Tony Lefebvre. OGT: a short overview of an enzyme standing out from usual glycosyltransferases. Biochemical Society Transactions, 2017, Biochemical Society Transactions, 45 (2), pp.365-370. ⟨10.1042/BST20160404⟩. ⟨hal-03167805⟩

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