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Literature summary for 2.3.1.48 extracted from

  • Karukurichi, K.R.; Wang, L.; Uzasci, L.; Manlandro, C.M.; Wang, Q.; Cole, P.A.
    Analysis of p300/CBP histone acetyltransferase regulation using circular permutation and semisynthesis (2010), J. Am. Chem. Soc., 132, 1222-1223.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information partial loop deletion or autoacetylation of up to 17 sites in p300 HAT leads to an increase in catalytic activity by 4-10fold Homo sapiens

Protein Variants

Protein Variants Comment Organism
Y1467F the mutant shows a 150fold reduction in catalytic activity relative to wild-type enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + histone H4 activity with synthetic histone H4 tail peptide substrate of p300 that shows different degrees of autoacetylation, overview. Tyr1467 appears to serve as a general acid protonating the departing coenzyme A sulfur Homo sapiens CoA + acetylhistone H4
-
?
additional information p300 performs autoacetylation, overview Homo sapiens ?
-
?

Synonyms

Synonyms Comment Organism
p300
-
Homo sapiens
p300 HAT
-
Homo sapiens
p300/CBP histone acetyltransferase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Homo sapiens