Is Dihydropteridine Reductase an Anomalous Dihydrofolate Reductase, a Flavin-Like Enzyme, or a Short-Chain Dehydrogenase?

  • John M. Whiteley
  • Nguyen H. Xuong
  • Kottayil I. Varughese
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 338)

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.

Keywords

Dihydrofolate Reductase Hydride Transfer Dihydropteridine Reductase Short Chain Dehydrogenase Folate Reductase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • John M. Whiteley
    • 1
  • Nguyen H. Xuong
    • 2
  • Kottayil I. Varughese
    • 1
    • 2
  1. 1.The Scripps Research InstituteLa JollaUSA
  2. 2.University of California at San DiegoLa JollaUSA

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