Thesis (M.Sc.) -- University of Toronto, 1996.
|Series||Canadian theses = -- Thèses canadiennes|
|The Physical Object|
|Pagination||2 microfiches : negative. --|
NAT2 coordinates from chain A (NAT2 protein 1) were used for these analyses because chain B (NAT2 protein 2) is missing coordinates of atoms for residue E and have more undetermined atoms than the chain A. None of the missing residues in chain A interact with any of the residues evaluated in this by: The crystal structure of human NAT1 and NAT2 proteins, three-dimensional modeling, and docking simulations have provided insights into the functional properties of the . Much of the groundwork for the determination of human NAT structures and functions was provided by seminal biochemical and enzyme kinetic studies in both human and non-human model systems, the cloning and primary amino acid sequence determination of eukaryotic and prokaryotic NATs, the characterization of naturally occurring and artificially mutated forms of human NATs, elucidation of the crystal structures of several prokaryotic NAT Cited by: The human arylamine N-acetyltransferases NATl and NAT2 catalyze the biotransformation of primary aro- matic amine or hydrazine drugs and xenobiotics. These.
Human N-acetyltransferase 1 (NAT1) alleles are characterized by one or more single nucleotide polymorphisms (SNPs) associated with rapid and slow acetylation phenotypes. NAT1 both activates and deactivates arylamine drugs and carcinogens, and NAT1 polymorphisms are associated with increased frequencies of many cancers and birth by: In these cells, stimulation with insulin decreased the mRNA levels of mouse Nat1 by approximately 50%, without an effect on mouse Nat2 (the ortholog to human NAT1) (ref. 21 and Supplemental Figure. The human arylamine N-acetyltransferase NAT2 is responsible for the biotransformation of numerous arylamine drugs and carcinogens.A common polymorphism of the NAT2 gene has been associated with susceptibility to drug toxicity and various malignancies. In this study, we used the crystal structure of the Salmonella typhimurium NAT (StNAT) to construct a high-quality model of a catalytic N Cited by: Dupret JM, Goodfellow GH, Janezic SA, Grant DM. Structure-function studies of human arylamine N-acetyltransferases NAT1 and NAT2. Functional analysis of recombinant NAT1/NAT2 chimeras expressed in Escherichia coli. J Biol Chem. Oct 28; (43)– Goodfellow GH, Dupret JM, Grant by:
Study of the role of the highly conserved residues Arg9 and Arg64 in the catalytic function of human N-acetyltransferases NAT1 and NAT2 by site-directed mutagenesis. Abstract. Human acetyl coenzyme A-dependent N-acetyltransferase (EC ) (NAT) catalyzes the biotransformation of a number of arylamine and hydrazine isozymes are encoded at 2 loci; one encodes NAT1, formerly known as the monomorphic form of the enzyme, while the other encodes the polymorphic NAT2, which is responsible for individual differences in the ability to Cited by: Human NAT1 and NAT2 genes were subcloned into pACYC vector and the plasmids thus obtained were introduced into Salmonella typhimurium O-acetyltransferase-deficient strain NM (TA/1,8-DNP/pSK), establishing new strains NM and NM, compared the sensitivities of these two strains with those of NM towards carcinogenic nitroarenes and Cited by: In humans NAT1 is located in the NAT cluster that comprises kb and includes two functional genes, NAT1 and NAT2. In other species the number of NAT genes range from 0 to 4. Structure of the human NAT1 gene and common NAT1 transcripts. Transcription: The human NAT1 gene has nine exons.