Enzyme

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     2. Transferases
        2.3 Acyltransferases
            2.3.1 Transferring groups other than aminoacyl groups
ID:2.3.1.5
Description:Arylamine N-acetyltransferase.
Alternative Name: Arylamine acetylase.
Cath: 3.30.2140.10; 3.30.2140.20; 3.40.630.30; 2.40.128.150;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.3.1.5
BRENDA Enzyme Link: BRENDA 2.3.1.5
KEGG Enzyme Link: KEGG2.3.1.5
BioCyc Enzyme Link: BioCyc 2.3.1.5
ExPASy Enzyme Link: ExPASy2.3.1.5
EC2PDB Enzyme Link: EC2PDB 2.3.1.5
ExplorEnz Enzyme Link: ExplorEnz 2.3.1.5
PRIAM enzyme-specific profiles Link: PRIAM 2.3.1.5
IntEnz Enzyme Link: IntEnz 2.3.1.5
MEDLINE Enzyme Link: MEDLINE 2.3.1.5
MSA:

2.3.1.5;

Phylogenetic Tree:

2.3.1.5;

Uniprot:
M-CSA:
RHEA:16613 acetyl-CoA + an arylamine = an N-acetylarylamine + CoA
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[S;H0;+0:6]-[*:7]>>[*:7]-[SH;+0:6].[*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance.Payton M, Auty R, Delgoda R, Everett M, Sim E1999 Feb9973365
Temperature stability of proteins essential for the intracellular survival of Mycobacterium tuberculosis.Lack NA, Kawamura A, Fullam E, Laurieri N, Beard S, Russell AJ, Evangelopoulos D, Westwood I, Sim E2009 Mar 119014350
Kinetic and chemical mechanism of arylamine N-acetyltransferase from Mycobacterium tuberculosis.Sikora AL, Frankel BA, Blanchard JS2008 Oct 718795795
The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid.Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M2002 May 1012054803