Disease relevance of Dhpr

• The recombinant DHPR protein expressed in Escherichia coli showed DHPR enzyme activity [1].

High impact information on Dhpr

• This result, coupled to the three-dimensional model built for Drosophila alcohol dehydrogenase, suggests a binding mechanism for the cofactor NAD different from that found for 3 alpha,20 beta-dehydroxysteroid dehydrogenase and similar to that found in the crystal structure of rat liver dihydropteridine reductase [2].
• The predicted amino acid sequence of the Drosophila DHPR protein was highly homologous to other species including human and mouse [1].
• In particular, the Tyr-(Xaa)(3)-Lys motif, known as the NAD(P)H binding domain, and most amino acids relevant to quinonoid dihydropteridine binding site are identical to human DHPR [1].
• Dihydropteridine reductase (DHPR) catalyzes the NAD(P)H-mediated reduction of quinonoid dihydropteridine as a part of pterin-dependent aromatic amino acid hydroxylation [1].
• 1. Pteridine cofactor of phenylalanine hydroxylase (EC 1.14.16.1) and dihydropteridine reductase (EC 1.6.99.7) in the phenylalanine hydroxylating system have been studied in the fetal rat liver [3].

Analytical, diagnostic and therapeutic context of Dhpr

• We isolated a fragment of Drosophila DHPR gene by PCR using degenerate primers [1].

References