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Information on EC 2.3.1.5 - arylamine N-acetyltransferase

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EC Tree
IUBMB Comments
Wide specificity for aromatic amines, including serotonin; also catalyses acetyl-transfer between arylamines without CoA.
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This record set is specific for:
UNIPROT: Q5YYQ3
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
serotonin n-acetyltransferase, arylamine n-acetyltransferase, arylamine n-acetyltransferase 1, arylamine n-acetyltransferase 2, tbnat, arylamine acetyltransferase, n-acetyltransferase a, nat 1, acetyl-coa:arylamine n-acetyltransferase, n-acetyltransferase type 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
arylamine N-acetyltransferase
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2-naphthylamine N-acetyltransferase
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-
-
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4-aminobiphenyl N-acetyltransferase
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-
-
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acetyl CoA-arylamine N-acetyltransferase
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-
-
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acetyltransferase, 2-naphthylamine N-
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-
-
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acetyltransferase, 4-aminobiphenyl
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-
-
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acetyltransferase, arylamine
-
-
-
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acetyltransferase, p-aminosalicylate N-
-
-
-
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acetyltransferase, procainamide N-
-
-
-
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acetyltransferase, serotonin N-
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-
-
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arylamine acetylase
-
-
-
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arylamine acetyltransferase
-
-
-
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beta-naphthylamine N-acetyltransferase
-
-
-
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indoleamine N-acetyltransferase
-
-
-
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N-acetyltransferase
-
-
-
-
NAT
-
-
-
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NAT1
-
-
-
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NAT2
-
-
-
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p-aminosalicylate N-acetyltransferase
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-
-
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serotonin acetyltransferase
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-
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serotonin N-acetyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
acetyl-CoA:arylamine N-acetyltransferase
Wide specificity for aromatic amines, including serotonin; also catalyses acetyl-transfer between arylamines without CoA.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-33-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetyl-CoA + 2-aminofluorene
CoA + N-acetyl-2-aminofluorene
show the reaction diagram
-
-
-
?
acetyl-CoA + 4-aminobenzoic acid
CoA + N-acetyl-4-aminobenzoic acid
show the reaction diagram
-
-
-
?
acetyl-CoA + 4-aminobiphenyl
CoA + N-acetyl-4-aminobiphenyl
show the reaction diagram
-
-
-
?
acetyl-CoA + 4-aminosalicylate
CoA + N-acetyl-4-aminosalicylate
show the reaction diagram
-
-
-
?
acetyl-CoA + 4-aminoveratrole
CoA + N-acetyl-4-aminoveratrole
show the reaction diagram
-
-
-
?
acetyl-CoA + 5-aminosalicylate
CoA + N-acetyl-5-aminosalicylate
show the reaction diagram
-
-
-
?
acetyl-CoA + benzidine
CoA + N-acetyl-benzidine
show the reaction diagram
-
-
-
?
acetyl-CoA + beta-naphthylamine
CoA + N-acetyl-beta-naphthylamine
show the reaction diagram
-
-
-
?
acetyl-CoA + hydralazine
CoA + N-acetyl-hydralazine
show the reaction diagram
-
-
-
?
acetyl-CoA + isoniazid
CoA + N-acetyl-isoniazid
show the reaction diagram
-
-
-
?
acetyl-CoA + sulfamethazine
CoA + N-acetyl-sulfamethazine
show the reaction diagram
-
-
-
?
acetyl-CoA + sulfamethoxazole
CoA + N-acetyl-sulfamethoxazole
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.414
isoniazid
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.013
substrate: 2-aminofluorene
0.015
substrate: sulfamethazine
0.023
substrate: beta-naphthylamine
0.024
substrate: 4-aminobiphenyl
0.02463
substrate: 5-aminosalicylate
0.029
substrate: sulfamethoxazole
0.052
substrate: benzidine
0.079
substrate: 4-aminoveratrole
0.087
substrate: hydralazine
0.111
substrate: 4-aminobenzoic acid
0.372
substrate: 4-aminosalicylate
2.878
substrate: isoniazid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q5YYQ3_NOCFA
Nocardia farcinica (strain IFM 10152)
293
0
32824
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of NfNAT is solved at a resolution of 2.7 A. Despite low sequence identity, enzyme shares an almost identical fold with that of other prokaryotic NATs, e.g. Mycobacterium smegmatis NAT and Mycobacterium marinum NAT. The overall NfNAT structure consists of three domains of equivalent size. The first two domains, a helical bundle (amino acids 1-98) and a beta-barrel (amino acids 99-199), are disposed in such a way that three residues (Cys82, His119, and Asp136) form a catalytic triad. The third domain is linked to the second through an interdomain helix (alpha6: amino acids 200-210). As shown for other prokaryotic NAT structures, the interface formed between domains 2 and 3 forms a substantial active-site cleft
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martins, M.; Pluvinage, B.; de la Sierra-Gallay, I.L.; Barbault, F.; Dairou, J.; Dupret, J.M.; Rodrigues-Lima, F.
Functional and structural characterization of the arylamine N-acetyltransferase from the opportunistic pathogen Nocardia farcinica
J. Mol. Biol.
383
549-560
2008
Nocardia farcinica, Nocardia farcinica (Q5YYQ3)
Manually annotated by BRENDA team