Design of Inhibitors of Orotidine Monophosphate Decarboxylase Using Bioisosteric Replacement and Determination of Inhibition Kinetics-Reference-Cited by-同舟云学术

Design of Inhibitors of Orotidine Monophosphate Decarboxylase Using Bioisosteric Replacement and Determination of Inhibition Kinetics

Published:2006-07-19 Issue:16 Volume:49 Page:4937-4945
ISSN:0022-2623
Container-title:Journal of Medicinal Chemistry
language:en
Short-container-title:J. Med. Chem.

Author:

Poduch Ewa¹,Bello Angelica M.¹,Tang Sishi¹,Fujihashi Masahiro¹,Pai Emil F.¹,Kotra Lakshmi P.¹

Affiliation:

1. Molecular Design and Information Technology Center, Leslie Dan Faculty of Pharmacy, University of Toronto, Toronto, Ontario M5S 2S2, Canada, Departments of Biochemistry, Medical Biophysics, and Molecular & Medical Genetics and Division of Cancer Genomics & Proteomics, Ontario Cancer Institute/Princess Margaret Hospital, Toronto, Ontario M5G 2M9, Canada, and Division of Cell and Molecular Biology, Toronto General Research Institute, University Health Network, Toronto, Ontario, M5G 2C4, Canada

Publisher

American Chemical Society (ACS)

Subject

Drug Discovery,Molecular Medicine

Link

https://pubs.acs.org/doi/pdf/10.1021/jm060202r

Reference42 articles.

1. A Proficient Enzyme

2. Purification and characterization of orotidine-5'-phosphate decarboxylase from Escherichia coli K-12.

3. Orotate phosphoribosyltransferase and orotidylate decarboxylase from Crithidia luciliae: Subcellular location of the enzymes and a study of substrate channeling

4. Computer simulations of enzyme catalysis: Finding out what has been optimized by evolution

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