1gte: Difference between revisions
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[[Category: pyrimidine catabolism]] | [[Category: pyrimidine catabolism]] | ||
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Revision as of 16:14, 30 October 2007
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DIHYDROPYRIMIDINE DEHYDROGENASE (DPD) FROM PIG, BINARY COMPLEX WITH 5-IODOURACIL
OverviewOverview
Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step, in pyrimidine degradation by converting pyrimidines to the corresponding, 5,6- dihydro compounds. The three-dimensional structures of a binary, complex with the inhibitor 5-iodouracil and two ternary complexes with, NADPH and the inhibitors 5-iodouracil and uracil-4-acetic acid were, determined by x-ray crystallography. In the ternary complexes, NADPH is, bound in a catalytically competent fashion, with the nicotinamide ring in, a position suitable for hydride transfer to FAD. The structures provide a, complete picture of the electron transfer chain from NADPH to the, substrate, 5-iodouracil, spanning a distance of 56 A and involving FAD, four [Fe-S] clusters, and FMN as cofactors. The crystallographic analysis, ... [(full description)]
About this StructureAbout this Structure
1GTE is a [Single protein] structure of sequence from [Sus scrofa] with SF4, FMN, FAD and IUR as [ligands]. Active as [Dihydropyrimidine dehydrogenase (NADP(+))], with EC number [1.3.1.2]. Structure known Active Site: FA1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the productive ternary complex of dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil. Implications for mechanism of inhibition and electron transfer., Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist Y, J Biol Chem. 2002 Apr 12;277(15):13155-66. Epub 2002 Jan 16. PMID:11796730
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