Silvio Garattini's Advances in Pharmacology and Chemotherapy Volume 17 PDF

By Silvio Garattini

ISBN-10: 0080581080

ISBN-13: 9780080581088

ISBN-10: 0120329174

ISBN-13: 9780120329175

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Extra resources for Advances in Pharmacology and Chemotherapy Volume 17

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37 41 41 45 50 50 57 66 68 74 76 80 80 83 86 87 87 87 90 91 91 92 92 92 93 94 . 1 Introduction Dihydrofolate reductase (DHFR) (tetrahydrofolate N A D P oxidoreductase. 5. 3) catalyzes the NADPH-dependent reduction of 7. 8. 7. tetrahydrofolate (THF) (see Fig . 1): DHF + NADPH + H+ THF + NADP (1) THF is a coenzyme in a number of 1-carbon transfer reactions (Rader and 37 Copyright 0 1980 by Academic Press.

The present degree of characterization of the enzyme structure should encourage more efforts in the future in rational synthesis of new drugs. The discussion begins with a review of critical aspects of enzyme structure as revealed by a comparison of the known amino acid sequences of a number of DHFRs and X-ray crystallographic studies on enzyme-inhibitor complexes. A major emphasis in this article will be in relating the biochemical and physicochemical evidence to these essential features of the enzyme and to the physicochemical properties of the substrate and inhibitor molecules themselves.

1975a). Comparison of the three bacterial sequences by Freisheim et al. (1978) 44 JILL E. GREADY showed that the L . casei enzyme sequence had 29 and 34% identities, respectively, with the E. coli and S . faecium enzymes. Comparison of the first 67 highly conserved residues indicated that L. casei and S . 55 whereas the analogous figures for L. caseilE. coli and E. colils. 88, respectively. , 1979). Also, with the exception of the COOH-terminal 30 or so amino acids, the residues which are common to the mammalian and bacterial enzymes are distributed throughout the lengths of the molecules, suggesting that all the enzymes have similar overall structures (see Section II,B for comments on E.

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Advances in Pharmacology and Chemotherapy Volume 17 by Silvio Garattini

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