OGT: a short overview of an enzyme standing out from usual glycosyltransferases.
Biochem Soc Trans
; 45(2): 365-370, 2017 04 15.
Article
em En
| MEDLINE
| ID: mdl-28408476
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Acetilglucosamina
/
Beta-N-Acetil-Hexosaminidases
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N-Acetilglucosaminiltransferases
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Biochem Soc Trans
Ano de publicação:
2017
Tipo de documento:
Article
País de afiliação:
França