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Literature summary extracted from

  • Chen, W.; Bacanamwo, M.; Harrison, D.G.
    Activation of p300 histone acetyltransferase activity is an early endothelial response to laminar shear stress and is essential for stimulation of endothelial nitric-oxide synthase mRNA transcription (2008), J. Biol. Chem., 283, 16293-16298.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.48 laminar shear stress laminar shear stress stimulates acetylation of histones 3 and 4 at the region of the eNOS promoter SSRE and extends 3' toward the eNOS coding region. Laminar shear stress induces p300 binding to p65 and leads to increase of p300 histone acetyltransferase activity by 2.5fold and to increase of acetylation of p65, but not of p50 acetylation, overview Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.48 curcumin increase in eNOS mRNA, caused by shear stress, is completely blocked by p300 small interfering RNA; increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.48 chromatin
-
Homo sapiens 785
-
2.3.1.48 nucleus
-
Homo sapiens 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.48 acetyl-CoA + histone H3 Homo sapiens
-
CoA + acetylhistone H3
-
?
2.3.1.48 acetyl-CoA + histone H4 Homo sapiens
-
CoA + acetylhistone H4
-
?
2.3.1.48 acetyl-CoA + p50 protein Homo sapiens acetylation of p50 by p300 independent of shear stress CoA + acetyl-p50 protein
-
?
2.3.1.48 acetyl-CoA + p65 protein Homo sapiens acetylation of p65 by p300 during translocation into the nuclei in response to shear stress CoA + acetyl-p65 protein
-
?
2.3.1.48 additional information Homo sapiens increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin or by p300 small interfering RNA ?
-
?

Organism

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.48 umbilical vein endothelial cell
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.48 acetyl-CoA + histone H3
-
Homo sapiens CoA + acetylhistone H3
-
?
2.3.1.48 acetyl-CoA + histone H4
-
Homo sapiens CoA + acetylhistone H4
-
?
2.3.1.48 acetyl-CoA + histone H4 substrate is H4 peptide Homo sapiens CoA + acetylhistone H4
-
?
2.3.1.48 acetyl-CoA + p50 protein acetylation of p50 by p300 independent of shear stress Homo sapiens CoA + acetyl-p50 protein
-
?
2.3.1.48 acetyl-CoA + p50 protein acetylation of histones H4 at the site of SSRE within the eNOS promoter Homo sapiens CoA + acetyl-p50 protein
-
?
2.3.1.48 acetyl-CoA + p65 protein acetylation of p65 by p300 during translocation into the nuclei in response to shear stress Homo sapiens CoA + acetyl-p65 protein
-
?
2.3.1.48 acetyl-CoA + p65 protein acetylation of histones H3 at the site of SSRE within the eNOS promoter Homo sapiens CoA + acetyl-p65 protein
-
?
2.3.1.48 additional information increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin or by p300 small interfering RNA Homo sapiens ?
-
?

Synonyms

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

Cofactor

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

General Information

EC Number General Information Comment Organism
2.3.1.48 physiological function p300 plays a key role in NFkappaB subunit acetylation Homo sapiens