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Literature summary for 2.3.1.48 extracted from

  • Lopez-Rodas, G.; Perez-Ortin, J.E.; Tordera, V.; Salvador, M.L.; Franco, L.
    Partial purification and properties of two histone acetyltransferases from the yeast, Saccharomyces cerevisiae (1985), Arch. Biochem. Biophys., 239, 184-190.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
DNA enzyme form A activated by low concentration, enzyme form B inhibited Saccharomyces cerevisiae

Inhibitors

Inhibitors Comment Organism Structure
DNA enzyme form A activated by low concentrations, enzyme form B inhibited Saccharomyces cerevisiae
p-chloromercuribenzoate enzyme form B less sensitive than enzyme form A Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
130000
-
 enzyme form B, gel filtration Saccharomyces cerevisiae
160000
-
 enzyme form A, gel filtration Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 enzyme form A and B
-

Purification (Commentary)

Purification (Comment) Organism
partial, enzyme form A and B Saccharomyces cerevisiae

Storage Stability

Storage Stability Organism
4°C, stable for several weeks Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + histone chicken erythrocyte histones, enzyme form A and B Saccharomyces cerevisiae CoA + acetylhistone
-
 ?
acetyl-CoA + histone H2B histone H2B: preferred substrate of enzyme form A Saccharomyces cerevisiae CoA + acetylhistone H2B
-
 ?
acetyl-CoA + histone H3 histone H3 preferred substrate of enzyme form A Saccharomyces cerevisiae CoA + acetylhistone H3
-
 ?
acetyl-CoA + histone H4 enzyme form B has a marked specificity for histone H4 Saccharomyces cerevisiae CoA + acetylhistone H4
-
 ?
acetyl-CoA + protamine sulfate enzyme form A, not enzyme form B Saccharomyces cerevisiae ?
-
 ?