Literature summary for 2.4.1.255 extracted from

Joiner, C.M.; Levine, Z.G.; Aonbangkhen, C.; Woo, C.M.; Walker, S.
Aspartate residues far from the active site drive O-GlcNAc transferase substrate selection (2019), J. Am. Chem. Soc., 141, 12974-12978 .

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Protein Variants

Protein Variants	Comment	Organism
D368A	activity is identical to wild-type enzyme	Homo sapiens
D386A/D420A	activity is 190% compared to wild-type enzyme	Homo sapiens
D386A/D420A/D454A	activity is 170% compared to wild-type enzyme	Homo sapiens
D4209A/D454A	activity is 80% compared to wild-type enzyme	Homo sapiens
D420A	activity is 130% compared to wild-type enzyme	Homo sapiens
D454A	activity is 130% compared to wild-type enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O15294	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	aspartate residues far from the active site drive O-GlcNAc transferase substrate selection	Homo sapiens	?	-	-

Synonyms

Synonyms	Comment	Organism
O-GlcNAc transferase	-	Homo sapiens
OGT	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	the enzyme is responsible for all nucleocytoplasmic O-GlcN acylation. Aspartate residues far from the active site drive O-GlcNAc transferase substrate selection	Homo sapiens

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Release 2023.1 (January 2023)