Structural highlights
Function
[DHPR_RAT] The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a binary complex of dihydropteridine reductase [DHPR; NAD(P)H:6,7-dihydropteridine oxidoreductase, EC 1.6.99.7] with its cofactor, NADH, has been solved and refined to a final R factor of 15.4% by using 2.3 A diffraction data. DHPR is an alpha/beta protein with a Rossmann-type dinucleotide fold for NADH binding. Insertion of an extra threonine residue in the human enzyme is associated with severe symptoms of a variant form of phenylketonuria and maps to a tightly linked sequence of secondary-structural elements near the dimer interface. Dimerization is mediated by a four-helix bundle motif (two helices from each protomer) having an unusual right-handed twist. DHPR is structurally and mechanistically distinct from dihydrofolate reductase, appearing to more closely resemble certain nicotinamide dinucleotide-requiring flavin-dependent enzymes, such as glutathione reductase.
Crystal structure of rat liver dihydropteridine reductase.,Varughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6080-4. PMID:1631094[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Varughese KI, Skinner MM, Whiteley JM, Matthews DA, Xuong NH. Crystal structure of rat liver dihydropteridine reductase. Proc Natl Acad Sci U S A. 1992 Jul 1;89(13):6080-4. PMID:1631094
