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Literature summary extracted from

  • Rodrigues-Lima, F.; Dupret, J.M.
    3D Model of human arylamine N-acetyltransferase 2: structural basis of the slow acetylator phenotype of the R64Q variant and analysis of the active-site loop (2002), Biochem. Biophys. Res. Commun., 291, 116-123.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.5 R64Q structural basis of the effects of the common genetic polymorphism on NAT2 activity, enzyme and active site structure analysis, phenotype, overview Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.5 acetyl-CoA + an arylamine Homo sapiens NAT2 is responsible for the biotransformation of numerous arylamine drugs and carcinogens CoA + an N-acetylarylamine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Homo sapiens P11245 NAT2; isozyme NAT2
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.5 acetyl-CoA + an arylamine = CoA + an N-acetylarylamine a conserved active site loop is involved in substrate recognition, structure analysis, Ser125 in NAT2 is proximal to the catalytic triad and faces a passageway to the catalytic core Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + an arylamine
-
 Homo sapiens CoA + an N-acetylarylamine
-
 ?
2.3.1.5 acetyl-CoA + an arylamine NAT2 is responsible for the biotransformation of numerous arylamine drugs and carcinogens Homo sapiens CoA + an N-acetylarylamine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.5 More construction of a high-quality model of a catalytic N-terminal region of NAT2, comprising residues 34-131, using the crystal structure of the Salmonella typhimurium NAT, PDB entry 1e2t, overview Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 NAT
-
 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.5 acetyl-CoA
-
 Homo sapiens