2DPG
COMPLEX OF INACTIVE MUTANT (H240->N) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH NADP+
Summary for 2DPG
| Entry DOI | 10.2210/pdb2dpg/pdb |
| Descriptor | GLUCOSE 6-PHOSPHATE DEHYDROGENASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | oxidoreductase, choh(d) - nad(p), nadp/nad, glucose metabolism |
| Biological source | Leuconostoc mesenteroides |
| Total number of polymer chains | 1 |
| Total formula weight | 55089.01 |
| Authors | Adams, M.J.,Naylor, C.E.,Paludin, S.,Gover, S. (deposition date: 1998-04-17, release date: 1998-07-15, Last modification date: 2024-04-03) |
| Primary citation | Cosgrove, M.S.,Naylor, C.,Paludan, S.,Adams, M.J.,Levy, H.R. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry, 37:2759-2767, 1998 Cited by PubMed Abstract: The catalytic mechanism of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides was investigated by replacing three amino acids, His-240, Asp-177, and His 178, with asparagine, using site-directed mutagenesis. Each of the mutant enzymes was purified to homogeneity and characterized by substrate binding studies and steady-state kinetic analyses. The three-dimensional structure of the H240N glucose 6-phosphate dehydrogenase was determined at 2.5 A resolution. The results support a mechanism in which His-240 acts as the general base that abstracts the proton from the C1-hydroxyl group of glucose 6-phosphate, and the carboxylate group of Asp-177 stabilizes the positive charge that forms on His-240 in the transition state. The results also confirm the postulated role of His-178 in binding the phosphate moiety of glucose 6-phosphate. PubMed: 9485426DOI: 10.1021/bi972069y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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