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Literature summary for 2.3.1.5 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

Protein Variants Comment Organism
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)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P11245 NAT2; isozyme NAT2
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Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
NAT
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Homo sapiens

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
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Homo sapiens