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Literature summary for 2.3.1.48 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

Inhibitors Comment Organism Structure
CoA competitive Rattus norvegicus
N6-Acetyllysine competitive Rattus norvegicus

KM Value [mM]

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

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rattus norvegicus

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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

Ki Value [mM]

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