Functional arginine residues involved in coenzyme binding by dihydrofolate reductase |
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Authors: | Gordon A Vehar James H Freisheim |
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Institution: | Department of Biological Chemistry, College of Medicine University of Cincinnati, Cincinnati, Ohio 45267 USA |
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Abstract: | Reaction of dihydrofolate reductase from amethopterin-resistant with phenylglyoxal results in a complete loss of enzyme activity. This inactivation is concomitant with the modification of five of a total of eight arginine residues per mole of enzyme. In the presence of the reduced coenzyme, NADPH, two of the five reactive arginines are protected from chemical modification with complete retention of enzyme activity. The results suggest the involvement of essential arginine residues at or near the coenzyme binding site and thus at or near the active center of the enzyme. |
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Keywords: | Research Career Development Awardee of the U S Public Health Service (CA-70449) to whom inquiries should be addressed |
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