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Literature summary 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

EC Number Activating Compound Comment Organism Structure
2.3.1.48 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

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.48 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.48 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
-
 ?
2.3.1.48 additional information p300 performs autoacetylation, overview Homo sapiens ?
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.48 acetyl-CoA
-
 Homo sapiens