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4 edition of Towards the generation and characterization of arylamine N-acetyltransferase-deficient mice found in the catalog.

Towards the generation and characterization of arylamine N-acetyltransferase-deficient mice

Hanan Abramovici

Towards the generation and characterization of arylamine N-acetyltransferase-deficient mice

by Hanan Abramovici

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Published by National Library of Canada in Ottawa .
Written in English


Edition Notes

Thesis (M.Sc.) -- University of Toronto, 2000.

SeriesCanadian theses = -- Thèses canadiennes
The Physical Object
FormatMicroform
Pagination2 microfiches : negative. --
ID Numbers
Open LibraryOL19333183M
ISBN 100612504484
OCLC/WorldCa51838539

  Click to launch & play an online audio visual presentation by Prof. Edith Sim on Arylamine N-acetyltransferases 1, part of a collection of online lectures. Human arylamine N-acetyltransferase 1 (NAT1) is a 33 kDa cytosolic protein with an active site catalytic triad (Sim et al., ). Both the crystal structure and the reaction kinetics (Fig. 1A and B) have been extensively reported (Rodrigues-Lima et al., ; Grant, ; Butcher andCited by: 7.

Mattano, S. S. et al. () Purification and biochemical characterization of hepatic arylamine N-acetyltransferase from rapid and slow acetylator mice: identity with arylhydroxamic acid N,O-acyltransferase and N-hydroxyarylamine O-acetyltransferase. Mol Pharmacol Arylamine N-acetyltransferase I (NAT1) is a phase II enzyme that acetylates a wide range of arylamine and hydrazine substrates. The NAT1 gene is located on chromosome 8 and shares homology to NAT genes found in most mammalian species. Gene expression occurs from at least two promoters and a number of tissue-specific transcripts have been Cited by:

Human arylamine N-acetyltransferase (NAT) is a phase II cytosolic enzyme that occurs as two isozymes, NAT1 and NAT2. This family of polymorphic enzymes catalyzes the detoxification and/or activation of many aromatic and heterocyclic amine drugs and carcinogens. These metabolism reactions can lead to detoxification of xenobiotics by N-acetylation, or bioactivation by O-acetylation which is Author: Carmine Simone Leggett. Abstract. Human arylamine N -acetyltransferase 1 (NAT1) is a widely distributed protein that has been implicated in a number of different cancers including brCited by:


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Towards the generation and characterization of arylamine N-acetyltransferase-deficient mice by Hanan Abramovici Download PDF EPUB FB2

Arylamine N-acetyltransferases (NATs) are polymorphic xenobiotic metabolising enzymes, linked to cancer susceptibility in a variety of tissues. In humans and in mice Cited by: Generation and Functional Characterization of Arylamine N-Acetyltransferase Nat1/Nat2Double-Knockout Mice Article (PDF Available) in Molecular Pharmacology 64(1).

Generation and functional characterization of arylamine N-acetyltransferase Nat1/Nat2 double-knockout mice. Mol Pharmacol – CrossRef, PubMed, CAS, Web of Science® Times Cited: 46; Sugamori KS, Brenneman D, Grant DM.

In vivo and in vitro metabolism of arylamine procarcinogens in acetyltransferase-deficient mice. Recent studies have revealed a possible link between the activities of polymorphic arylamine N‐acetyltransferases (NATs) and energy used a Nat1/Nat2 double knockout (KO) mouse model to demonstrate that ablation of the two Nat genes is associated with modest, intermittent alterations in respiratory exchange rate.

Pyruvate tolerance tests show that double KO mice Author: Raphaël G.P. Denis, Florent Busi, Julien Castel, Chloé Morel, Wenchao Zhang, Wenchao Zhang, Linh‐Chi.

Generation and analysis of mice with a targeted disruption of the arylamine N-acetyltransferase Type 2 Gene Article (PDF Available) in The Pharmacogenomics Journal 3(3) February Arylamine N-acetyltransferases (NATs) are well known as polymorphic Phase II drug-metabolizing enzymes, and catalyse the conjugation of an acetyl group from acetyl CoA onto an amine, hydrazine or hydroxylamine moiety of an aromatic compound reached prominence initially as one of the first enzymes to be recognized as a cause of interindividual variation in drug by: Chung, J.G.: Purification and characterization of an arylamine N-acetyltransferase in the nematode Enterobius vermicularis.

Microbios, 98, 15–25 () PubMed Google Scholar [41]. Known arylamine N-acetyltransferases (ECNAT) catalyze the transfer of an acetyl group from acetyl-CoA to the amino group of hydrazine, arylamine drugs, and of humans, mice, and intestinal microorganisms have been characterized 1., Human NAT I possibly plays a role in the activation of various carcinogens and in the metabolism of the folate catabolite p Cited by: 6.

Arylamine N-acetyltransferases (NATs, E.C. ) are a family of enzymes (30–34 kDa) found in a range of eukaryotes and catalyse the transfer of an acetyl group from a donor, such as acetyl coenzyme A (AcCoA) to an aromatic or heterocyclic amine, hydrazine, hydrazide or N-hydroxylamine acceptor substrate.

The NAT enzymes in prokaryotes, particularly NAT from S Cited by: The arylamine N-acetyltransferases (NATs; EC ) are Phase II Enzymes that catalyze the transfer of an acetyl group from acetyl coenzyme A to aromatic amine, heterocyclic amine, or hydrazine ation catalyzed by NATs is an important biotransformation pathway for many drugs and cancer, causing agents that we are exposed to on a daily basis.

Sugamori KS, Wong S, Gaedigk A, Yu V, Abramovici H, Rozmahel R, Grant DM. Generation and functional characterization of arylamine N-acetyltransferase Nat1/Nat2 double-knockout mice.

Molecular Pharmacology. ; – Wakefield L, Cornish V, Broackes-Carter F, Sim E. Arylamine N-acetyltransferase 2 expression in the developing by:   The University of Queensland's institutional repository, UQ eSpace, aims to create global visibility and accessibility of UQ’s scholarly : Neville J.

Butcher, Rodney F. Minchin. Arylamine N -acetyltransferases (NATs) catalyze the biotransformation of a variety of arylamine drugs and carcinogens and may play diametrically opposing roles in enhancing either the detoxification of these chemicals or their metabolic activation into DNA-binding electrophiles.

To facilitate the study of these processes, we have generated a Nat1 / Nat2 double-knockout mouse model by Cited by: THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol.

No. 17, Issue of Septem pp. Printed in U.S.A. Arylamine N-Acetyltransferase and Arylalkylamine N-Acetyltransferase in the Mammalian Pineal Gland* (Received for publication, February 1, ) Pierre Voisin, M.A. REVIEW Arylamine N-acetyltransferases: from drug metabolism and pharmacogenetics to drug discovery E Sim1,2, A Abuhammad2,3 and A Ryan1 1Faculty of Science Engineering and Computing, Kingston University, Kingston, UK, 2Department of Pharmacology, Oxford University, Oxford, UK, and 3Faculty of Pharmacy, University of Jordan, Amman, Jordan Correspondence Professor Edith Sim, Cited by:   Sugamori KS, Wong S, Gaedigk A, Yu V, Abramovici H, Rozmahel R, et al.

Generation and functional characterization of arylamine N-acetyltransferase Nat1/Nat2 double-knockout mice. Mol Pharmacol. ; –Cited by:   Mycolic acids represent a major component of the unique cell wall of mycobacteria.

Mycolic acid biosynthesis is inhibited by isoniazid, a key frontline antitubercular drug that is inactivated by mycobacterial and human arylamine N-acetyltransferase (NAT).We show that an in-frame deletion of Mycobacterium bovis BCG nat results in delayed entry into log phase, altered morphology, altered cell Cited by:   Arylamine N-acetyltransferase (NAT) genes in humans and in rodents encode polymorphic drug metabolizing NAT1 (and the murine equivalent mouse Nat2) is found early in embryonic development and is likely to have an endogenous role.

We report the detailed expression of the murine gene (Nat2) and encoded protein in mouse embryos, using a transgenic. Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Isoniazid, 2-aminofluorene and anisidine are preferred substrates for NAT No activity with p-aminobenzoic acid (PABA) nor SMZ.

The acetyl coenzyme A (AcCoA):arylamine N-acetyltrans-ferases (NAT; EC ) catalyze the transfer of an acetyl group from AcCoA to the nitrogen or oxygen atom of primary arylamines, hydrazines, and their N-hydroxylated metabolites. They therefore play important roles in both the detoxification and metabolic activation of numerous xenobiotics.

Chagas disease is a neglected tropical disease with 6–7 million people infected worldwide, and there is no effective treatment. Therefore, there is an urgent need to continue researching in order to discover novel therapeutic alternatives. We present a series of arylaminoketone derivatives as means of identifying new drugs to treat Chagas disease in the acute phase with greater activity Cited by: Clicking the images or links will redirect you to a website hosted by BenchSci that provides third-party scientific content.

Neither the content nor the BenchSci technology and processes for selection have been evaluated by us; we are providing them as-is and without warranty of any kind, including for use or application of the Thermo Fisher Scientific products presented.studies on human arylamine n-acetyltransferases a thesis submitted to the faculty of graduate school of the university of minnesota by li liu in partial fulfillment of the requirements for the degree of doctor of philosophy dr.

patrick e. hanna, advisor january,