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Literature summary extracted from

  • Stepp, M.W.; Mamaliga, G.; Doll, M.A.; States, J.C.; Hein, D.W.
    Folate-dependent hydrolysis of acetyl-coenzyme A by recombinant human and rodent arylamine N-acetyltransferases (2015), Biochem. Biophys. Rep., 3, 45-50.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.5 expressed in Escherichia coli JM105 cells Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.5 0.0543
-
 acetyl-CoA isoform NAT1, at 37°C, pH not specified in the publication Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + 4-aminobenzoate
-
 Homo sapiens CoA + N-acetyl-4-aminobenzoate
-
 ?
2.3.1.5 additional information isoform NAT1 catalyzes acetyl-CoA hydrolysis in a folate-dependent manner, while isoform NAT2 does not Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 NAT1 isoform Homo sapiens
2.3.1.5 NAT2 isoform Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.5 folate isoform NAT1 catalyzes acetyl-CoA hydrolysis in a folate-dependent manner, while isoform NAT2 does not Homo sapiens