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Literature summary extracted from

  • Wiktorowicz, J.E.; Campos, K.L.; Bonner, J.
    Substrate and product inhibition initial rate kinetics of histone acetyltransferase (1981), Biochemistry, 20, 1464-1467.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.48 CoA competitive Rattus norvegicus
2.3.1.48 N6-Acetyllysine competitive Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.48 additional information
-
 additional information
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.48 nucleus
-
 Rattus norvegicus 5634
-

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.48 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.48
-
 Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.48 acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine rapid equilibrium ordered bireactant mechanism Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.48 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.48 acetyl-CoA + histone
-
 Rattus norvegicus CoA + acetylhistone
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.48 1.96
-
 N6-Acetyllysine complexed with acetyl-CoA, versus histone Rattus norvegicus
2.3.1.48 2.5
-
 N6-Acetyllysine complexed with histone, versus acetyl-CoA Rattus norvegicus
2.3.1.48 2.77
-
 coenzyme A complexed with acetyl-CoA, versus histone Rattus norvegicus
2.3.1.48 5.43
-
 coenzyme A
-
 Rattus norvegicus