1e2t
From Proteopedia
Arylamine N-acetyltransferase (NAT) from Salmonella typhimurium
Structural highlights
FunctionNHOA_SALTY Catalyzes both the acetyl-CoA-dependent N-acetylation of aromatic amines and the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the O-acetylation of N-hydroxy-Glu-P-1, and the N-acetylation of isoniazid and 2-aminofluorene.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEnzymes of the arylamine N-acetyltransferase (NAT) family are found in species ranging from Escherichia coli to humans. In humans they are known to be responsible for the acetylation of a number of arylamine and hydrazine drugs, and they are strongly linked to the carcinogenic potentiation of certain foreign substances. In prokaryotes their substrate specificities may vary and members of the gene family have been linked to pathways including amide synthesis during rifamycin production. Here we report the crystal structure at 2.8 A resolution of a representative member of this family from Salmonella typhimurium in the presence and absence of a covalently bound product analog. The structure reveals surprising mechanistic information including the presence of a Cys-His-Asp catalytic triad. The fold can be described in terms of three domains of roughly equal length with the second and third domains linked by an interdomain helix. The first two domains, a helical bundle and a beta-barrel, make up the catalytic triad using a structural motif identical to that of the cysteine protease superfamily. Structure of arylamine N-acetyltransferase reveals a catalytic triad.,Sinclair JC, Sandy J, Delgoda R, Sim E, Noble ME Nat Struct Biol. 2000 Jul;7(7):560-4. PMID:10876241[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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