Literature summary for 2.3.1.48 extracted from

Toleman, C.; Paterson, A.J.; Whisenhunt, T.R.; Kudlow, J.E.
Characterization of the histone acetyltransferase (HAT) domain of a bifunctional protein with activable O-GlcNAcase and HAT activities (2004), J. Biol. Chem., 279, 53665-53673.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
acetyl-CoA + histone	Mus musculus	the bifunctional enzyme NCOAT, nuclear cytoplasmic O-GlcNacase and acetyltransferase, may be regulated to reduce the state of glycosylation of transcriptional activators while increasing the acetylation of histones to allow for concerted activation of eukaryotic gene transcription	CoA + acetylhistone	-	?

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q9EQQ9	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetyl-CoA + histone	the bifunctional enzyme NCOAT, nuclear cytoplasmic O-GlcNacase and acetyltransferase, may be regulated to reduce the state of glycosylation of transcriptional activators while increasing the acetylation of histones to allow for concerted activation of eukaryotic gene transcription	Mus musculus	CoA + acetylhistone	-	?

Synonyms

Synonyms	Comment	Organism
NCOAT	nuclear cytoplasmic O-GlcNacase and acetyltransferase, bifunctional enzyme	Mus musculus

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Release 2023.1 (January 2023)