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Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 3 | Page No.: 370-378
DOI: 10.3923/jbs.2005.370.378
Interaction of 2-thio-4-oxo-quinazoline Derivatives with Guinea Pig Liver Molybdenum Hydroxylases, Xanthine Oxidase and Aldehyde Oxidase
M. A. Al-Omar, S. T. Al-Rashood, H. I. El-Subbagh and S. G. Abdel Hamide

Abstract: Aldehyde oxidase and xanthine oxidase are molybdenum-containing enzymes distributed throughout animal kingdom. Aldehyde oxidase has a wide range of substrates including aldehydes and N-heterocycles while xanthine oxidase involves in oxidation of purine analogues to corresponding uric acid. In addition to cytochrome P450 isoenzymes, molybdenum hydroxylases are major defense mechanism for the removal of drugs/xenobiotics from the body. Fifty quinazoline derivatives have been synthesized and characterized by NMR infrared, mass spectrum and elementary analyses. These substituted quinazolines have been examined for their interaction with mol ybdenum hydroxylases and found to be weak inhibitor. They inhibit both enzymes in a competitive pattern with inhibitor constants (Ki) values ranging from 90-1200 μM. The relationship between Ki and relative lipophilicity of quinazolines, as inhibitors of molybdenum hydroxylase enzymes, has been compared. The specific-site of interaction and inhibitory potency of quinazolines on molybdenum hydroxylase have been discussed in this study.

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How to cite this article
M. A. Al-Omar, S. T. Al-Rashood, H. I. El-Subbagh and S. G. Abdel Hamide, 2005. Interaction of 2-thio-4-oxo-quinazoline Derivatives with Guinea Pig Liver Molybdenum Hydroxylases, Xanthine Oxidase and Aldehyde Oxidase. Journal of Biological Sciences, 5: 370-378.

Keywords: xanthine oxidase, aldehyde oxidase, Quinazolines dervatives and molybdenum hydroxylases

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