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Literature summary extracted from

  • Laurieri, N.; Dairou, J.; Egleton, J.E.; Stanley, L.A.; Russell, A.J.; Dupret, J.M.; Sim, E.; Rodrigues-Lima, F.
    From arylamine N-acetyltransferase to folate-dependent acetyl CoA hydrolase: impact of folic acid on the activity of (HUMAN)NAT1 and its homologue (MOUSE)NAT2 (2014), PLoS ONE, 9, e96370.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.5 N-[3-(3,5-dimethylanilino)-1,4-dioxo-1,4-dihydronaphthalen-2-yl]benzenesulfonamide selective competitive inhibitor Homo sapiens
2.3.1.5 N-[3-(3,5-dimethylanilino)-1,4-dioxo-1,4-dihydronaphthalen-2-yl]benzenesulfonamide selective competitive inhibitor Mus musculus
3.1.2.1 naphthoquinone
-
 Homo sapiens
3.1.2.1 naphthoquinone
-
 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.5 Homo sapiens
-
-
-
2.3.1.5 Mus musculus
-
-
-
3.1.2.1 Homo sapiens
-
-
-
3.1.2.1 Mus musculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.2.1 acetyl-CoA + H2O = CoA + acetate as shown by proton nuclear magnetic resonance spectroscopy the disappearance of acetyl CH3 from acetyl Coenzyme A occurres concomitantly with the appearance of a CH3 peak corresponding to that of free acetate and suggesting that folate is not acetylated during the reaction Mus musculus
a
3.1.2.1 acetyl-CoA + H2O = CoA + acetate as shown by proton nuclear magnetic resonance spectroscopy the disappearance of acetyl CH3 from acetyl Coenzyme A occurrs concomitantly with the appearance of a CH3 peak corresponding to that of free acetate and suggesting that folate is not acetylated during the reaction Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.5 acetyl-CoA + 4-aminobenzoate
-
 Mus musculus CoA + N-acetyl-4-aminobenzoate
-
 ?
2.3.1.5 acetyl-CoA + 4-aminobenzoate
-
 Homo sapiens CoA + N-acetyl-4-aminobenzoate
-
 ?
2.3.1.5 acetyl-CoA + N-(4-aminobenzoyl)-L-glutamate
-
 Mus musculus CoA + N-(4-acetylaminobenzoyl)-L-glutamate
-
 ?
2.3.1.5 acetyl-CoA + N-(4-aminobenzoyl)-L-glutamate
-
 Homo sapiens CoA + N-(4-acetylaminobenzoyl)-L-glutamate
-
 ?
3.1.2.1 acetyl-CoA + H2O
-
 Mus musculus CoA + acetate
-
 ?
3.1.2.1 acetyl-CoA + H2O
-
 Homo sapiens CoA + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.5 arylamine N-acetyltransferase type 1
-
 Homo sapiens
2.3.1.5 arylamine N-acetyltransferase type 2
-
 Mus musculus
2.3.1.5 NAT1
-
 Homo sapiens
2.3.1.5 NAT2
-
 Mus musculus
3.1.2.1 (HUMN)NAT1
-
 Homo sapiens
3.1.2.1 (MOUSE)NAT2
-
 Mus musculus
3.1.2.1 human arylamine N-acetyltransferase Type 1
-
 Homo sapiens
3.1.2.1 mouse arylamine N-acetyltransferase Type 2
-
 Mus musculus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.2.1 37
-
 assay at Mus musculus
3.1.2.1 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.2.1 7.5
-
 assay at Mus musculus
3.1.2.1 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.5 folate
-
 Mus musculus
2.3.1.5 folate
-
 Homo sapiens
3.1.2.1 folate folate binds at the enzyme's active site, and facilitate acetyl coenzyme A hydrolysis Mus musculus
3.1.2.1 folate folate binds at the enzyme's active site, and facilitate acetyl coenzyme A hydrolysis Homo sapiens