NDLI: Structural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases.

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Structural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases.

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Structural and mechanistic characteristics of dihydropteridine reductase: a member of the Tyr-(Xaa)3-Lys-containing family of reductases and dehydrogenases.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Xuong, N. H. Matthews, D. A. Varughese, K. I. Whiteley, J. M. Kiefer, P. M.
Description	Author Affiliation: Varughese KI ( University of California at San Diego, La Jolla 92093-0317.);
Abstract	Dihydropteridine reductase (EC 1.6.99.7) is a member of the recently identified family of proteins known as short-chain dehydrogenases. When the x-ray structure of dihydropteridine reductase is correlated with conserved amino acid sequences characteristic of this enzyme class, two important common structural regions can be identified. One is close to the protein N terminus and serves as the cofactor binding site, while a second conserved feature makes up the inner surface of an alpha-helix in which a tyrosine side chain is positioned in close proximity to a lysine residue four residues downstream in the sequence. The main function of this Tyr-Lys couple may be to facilitate tyrosine hydroxyl group participation in proton transfer. Thus, it appears that there is a distinctive common mechanism for this group of short-chain or pyridine dinucleotide-dependent oxidoreductases that is different from their higher molecular weight counterparts.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	12
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Dihydropteridine Reductase Chemistry Amino Acid Sequence Animals Catalysis Models, Molecular Molecular Sequence Data Protein Structure, Tertiary Sequence Alignment Sequence Homology, Amino Acid Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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