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Literature summary for 2.3.1.48 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
Search for more literature for 2.3.1.48

Inhibitors

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

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
from calf Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
thymus
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
acetyl-CoA + histone H2A enzyme form B nearly exclusively acetylates histones H4 and H2a Bos taurus CoA + acetylhistone H2A
-
 ?
acetyl-CoA + histone H4 enzyme form B nearly exclusively acetylates histones H4 and H2a Bos taurus CoA + acetylhistone H4
-
 ?