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Literature summary for 2.3.1.48 extracted from

  • Mingarro, I.; Sendra, R.; Salvador, M.L.; Franco, L.
    Site specificity of pea histone acetyltransferase B in vitro (1993), J. Biol. Chem., 268, 13248-13252.
    View publication on PubMed
Search for more literature for 2.3.1.48

Inhibitors

Inhibitors Comment Organism Structure
DNA
-
 Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm enzyme form B Pisum sativum 5737
-

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 enzyme form B
-
Pisum sativum
-
 cv. Lincoln
-

Purification (Commentary)

Purification (Comment) Organism
partial, enzyme form B Pisum sativum

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine acetylation of lysine 5, 8, 12, and 16 of free histone H4 Pisum sativum
a

Source Tissue

Source Tissue Comment Organism Textmining
seedling axe Pisum sativum
-
seedling i.e. embryo Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 acetyl-CoA + histone H4
-
 Pisum sativum 2 CoA + diacetylhistone H4 mono-, di- and triacetylated products ?
3 acetyl-CoA + histone H4 enzyme form B Pisum sativum 3 CoA + triacetylhistone H4 mono-, di- and triacetylated products ?
acetyl-CoA + histone free pea and chicken histones H4, enzyme form B Pisum sativum CoA + acetylhistone
-
 ?
acetyl-CoA + histone acetylation of lysine 5, 8, 12, and 16 of free histone H4 with increasing preference Pisum sativum CoA + acetylhistone
-
 ?
acetyl-CoA + histone H4 enzyme form B Pisum sativum CoA + acetylhistone H4 mono-, di- and triacetylated products ?