Disease relevance of C05649

• Isolation and characterization of dihydropteridine reductase from Pseudomonas species [1].
• The enzyme has no pteridine-independent oxidoreductase activity, in contrast to Escherichia coli dihydropteridine reductase, and thus appears more similar to mammalian dihydropteridine reductases, which do not contain a flavin prosthetic group [2].
• Production of antibodies to sheep liver dihydropteridine reductase: characterization and use to study the enzyme defect in a variant form of phenylketonuria [3].

High impact information on C05649

• Gel filtration of bovine liver extract on a Sephadex G-200 column resolved three macromolecular fractions with dihydropteridine reductase-dependent cytochrome c reducing activity [4].
• The kinetics of the reduction of quinonoid 2-amino-4-hydroxy-6, 7-dimethyldihydropteridine (DMPH2) catalyzed by bovine liver dihydropteridine reductase were examined with NADH, (S)-NADD, (S)-NADT, and [3H]-NADH as substrates [5].
• Immunochemical experiments using antibodies against bovine liver dihydropteridine reductase suggest that normal leukocytes and skin fibroblasts contain dihydropteridine reductase which is immunologically similar to that of human liver [6].
• Bovine dihydropteridine reductase: purification by affinity chromatography and comparison of enzymes from liver and adrenal medulla [7].
• Structural genomics of Caenorhabditis elegans: structure of dihydropteridine reductase [8].

Biological context of C05649

• 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 [9].

Analytical, diagnostic and therapeutic context of C05649

• The purification of rat and sheep liver dihydropteridine reductases by affinity chromatography on methotrexate-sepharose [10].
• Dihydropteridine reductase from bovine liver. Purification, crystallization, and isolation of a binary complex with NADH [11].

References