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Literature summary for 2.3.1.5 extracted from

  • Glowinski, I.B.; Weber, W.W.; Fysh, J.M.; Vaught, J.B.; King, C.M.
    Evidence that arylhydroxamic acid N,O-acyltransferase and the genetically polymorphic N-acetyltransferase are properties of the same enzyme in rabbit liver (1980), J. Biol. Chem., 255, 7883-7890.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Oryctolagus cuniculus 5829
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33000
-
gel filtration Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
slow and fast acetylator phenotype
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.145
-
2-aminofluorene Oryctolagus cuniculus
0.177
-
sulfamethazine Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 2-aminofluorene
-
Oryctolagus cuniculus CoA + 2-acetylaminofluorene
-
?
acetyl-CoA + 4-aminobenzoic acid
-
Oryctolagus cuniculus CoA + 4-acetylaminobenzoic acid
-
?
acetyl-CoA + sulfamethazine
-
Oryctolagus cuniculus CoA + N-4-acetylsulfamethazine
-
?

Subunits

Subunits Comment Organism
monomer 1 * 33000, SDS-PAGE Oryctolagus cuniculus