Structural highlights
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 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.
On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.,Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:9485426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR. On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase. Biochemistry. 1998 Mar 3;37(9):2759-67. PMID:9485426 doi:10.1021/bi972069y
