1h9a: Difference between revisions
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[[Category: oxidoreductase (choh(d) - nad(p))]] | [[Category: oxidoreductase (choh(d) - nad(p))]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:32:41 2007'' | ||
Revision as of 16:27, 30 October 2007
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COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L. MESENTEROIDES WITH COENZYME NADP
OverviewOverview
The reduced coenzymes NADH and NADPH only differ by one phosphate, but in, the cell NADH provides reducing power for catabolism while NADPH is, utilized in biosynthetic pathways. Enzymes almost invariably discriminate, between the coenzymes, but glucose 6-phosphate dehydrogenase (G6PD) from, Leuconostoc mesenteroides is rare in being functionally dual specific. In, order to elucidate the coenzyme selectivity, the structures of NADP(+)-, and NAD(+)-complexed L. mesenteroides G6PD have been determined including, data to 2.2 and 2.5 A resolution, respectively, and compared with, unliganded G6PD crystallized in the same space groups. Coenzyme binding is, also compared with that in a ternary complex of a mutant in which Asp177, in the active site has been mutated to asparagine. There are no ... [(full description)]
About this StructureAbout this Structure
1H9A is a [Single protein] structure of sequence from [Leuconostoc mesenteroides] with SO4 and NAP as [ligands]. Active as [Glucose-6-phosphate 1-dehydrogenase], with EC number [1.1.1.49]. Structure known Active Sites: NDP and SUL. Full crystallographic information is available from [OCA].
ReferenceReference
NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes., Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):635-48. Epub 2001, Apr 24. PMID:11320304
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