2pqt
Human N-acetyltransferase 1
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OverviewOverview
The human arylamine N-acetyltransferases NAT1 and NAT2 play an important, role in the biotransformation of a plethora of aromatic amine and, hydrazine drugs. They are also able to participate in the bioactivation of, several known carcinogens. Each of these enzymes is genetically variable, in human populations, and polymorphisms in NAT genes have been associated, with various cancers. Here we have solved the high resolution crystal, structures of human NAT1 and NAT2, including NAT1 in complex with the, irreversible inhibitor 2-bromoacetanilide, a NAT1 active site mutant, and, NAT2 in complex with CoA, and have refined them to 1.7-, 1.8-, and 1.9-A, resolution, respectively. The crystal structures reveal novel structural, features unique to human NATs and provide insights into the structural, basis of the substrate specificity and genetic polymorphism of these, enzymes.
About this StructureAbout this Structure
2PQT is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Arylamine N-acetyltransferase, with EC number 2.3.1.5 Full crystallographic information is available from OCA.
ReferenceReference
Structural Basis of Substrate-binding Specificity of Human Arylamine N-Acetyltransferases., Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN, J Biol Chem. 2007 Oct 12;282(41):30189-97. Epub 2007 Jul 26. PMID:17656365
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