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NATURAL PRODUCT INHIBITION STUDIES WITH NAD SYNTHETASE. Brandon S. Pybus, Dept. of Chemistry, Univ. of Ala. Birmingham, AL 35294. Erica R. Lawton, Dept. of Chemistry, Univ. of Tenn. Martin, TN. Christie G. Brouillette and Lawrence J. DeLucas, CBSE, Univ. of Ala. Birmingham, AL 35294. Donald D. Muccio, Dept. of Chemistry, Univ of Ala. Birmingham, AL 35294.

NAD synthetase, a member of the ATP pyrophosphatase family of enzymes, catalyzes the last step of the biosynthesis of nicotinamide adenine dinucleotide (NAD) from deamido nicotinamide adenine dinucleotide (NaAD), using the chemical energy in ATP.

MgATP + NaAD + NH3 [leftarrow / right arrow] [NAD.sup.+] + AMP + MgPPi

NAD Synthetase is considered a goad drug target for possible antibacterial drugs. The X-ray crystal structure shows that the enzyme exists as a homodimer, consisting of 30 kDa subunits. From enzyme kinetic data, enzyme-substrate dissociation constants and interactivity constants between substrates were determined. Inhibition studies then were carried Out with the natural products of this enzyme-mediated reaction. AMP displayed mixed (noncompetitive) type inhibition against all substrates as did PPi. This information reduced the total number of kinetic models from nineteen to five. Similar experiments are now under way with [NAD.sup.+]. Together these data will help refine the choice of kinetic mechanism for NAD Synthetase and further our understanding of the enzyme.
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Publication:Journal of the Alabama Academy of Science
Article Type:Brief Article
Geographic Code:1USA
Date:Jan 1, 2000
Previous Article:Yi-Chien Lee.

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