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Literature summary extracted from

  • Sures, I.; Gallwitz, D.
    Histone-specific acetyltransferases from calf thymus. Isolation, properties, and substrate specificity of three different enzymes (1980), Biochemistry, 19, 943-951.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.48 iodoacetamide enzyme form A is more sensitive than enzyme form B Bos taurus
2.3.1.48 N-ethylmaleimide enzyme form A is more sensitive than enzyme form B Bos taurus
2.3.1.48 p-chloromercuribenzoate
-
Bos taurus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.48 98000
-
enzyme form B, gel filtration Bos taurus
2.3.1.48 120000
-
enzyme form A, gel filtration Bos taurus
2.3.1.48 200000
-
above, enzyme form C, gel filtration Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.48 Bos taurus
-
calf
-
2.3.1.48 Bos taurus
-
3 enzyme forms: A, B, C
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.48 from calf Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.48 thymus
-
Bos taurus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.48 acetyl-CoA + histone enzyme form B nearly exclusively acetylates histones H4 and H2a Bos taurus CoA + acetylhistone formation of N6-acetyllysine as the only acetylation product ?
2.3.1.48 acetyl-CoA + histone H2A enzyme form B nearly exclusively acetylates histones H4 and H2a Bos taurus CoA + acetylhistone H2A
-
?
2.3.1.48 acetyl-CoA + histone H4 enzyme form B nearly exclusively acetylates histones H4 and H2a Bos taurus CoA + acetylhistone H4
-
?