Literature summary for 2.4.1.255 extracted from

Martin, S.E.S.; Tan, Z.W.; Itkonen, H.M.; Duveau, D.Y.; Paulo, J.A.; Janetzko, J.; Boutz, P.L.; Toerk, L.; Moss, F.A.; Thomas, C.J.; Gygi, S.P.; Lazarus, M.B.; Walker, S.
Structure-based evolution of low nanomolar O-GlcNAc transferase inhibitors (2018), J. Am. Chem. Soc., 140, 13542-13545 .

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Inhibitors

Inhibitors	Comment	Organism	Structure
ethyl (R)-4-(2-(2-((2-ethoxy-2-oxoethyl)(thiophen-2-ylmethyl)amino)-2-oxo-1-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)ethyl)phenoxy)butanoate	-	Homo sapiens
ethyl (R)-N-(2-((7-chloro-2-oxo-1,2-dihydroquinoline)-6-sulfonamido)-2-(2-methoxyphenyl)acetyl)-N-(thiophen-2-ylmethyl)glycinate	-	Homo sapiens
methyl (R)-N-(2-(2-methoxyphenyl)-2-((2-oxo-1,2-dihydroquinoline)-6-sulfonamido)acetyl)-N-(thiophen-2-ylmethyl)glycinate	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293T cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
O-linked N-acetylglucosamine transferase	-	Homo sapiens
OGT	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the enzyme is responsible for all nucleocytoplasmic glycosylation	Homo sapiens

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Release 2023.1 (January 2023)