Abstract
Dihydropteridine reductase (DHPR, EC 1.6.99.10) and dihydrofolate reductase (DHFR, EC 1.5.1.3) both employ a reduced dinucleotide cofactor to convert a dihydro pteridine substrate to a tetrahydropteridine product. In the former case the substrate has a quinonoid dihydro structure whereas in the latter the 7,8-dihydro form is the substrate. The quinonoid form resembles a flavin molecule and the enzymatic mechanism of reduction has common features to this latter class of compound. Additionally, DHPR contains a specific Tyr XXX Lys motif in its sequence that allows comparison with a class of short chain dehydrogenases.1 The relationship of DHPR to these differing enzymatic types is illustrated briefly in the following discussion.
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Whiteley, J.M., Xuong, N.H., Varughese, K.I. (1993). Is Dihydropteridine Reductase an Anomalous Dihydrofolate Reductase, a Flavin-Like Enzyme, or a Short-Chain Dehydrogenase?. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_23
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_23
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