1e77
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COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM LEUCONOSTOC MESENTEROIDES WITH SUBSTRATE
OverviewOverview
The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate, dehydrogenase from Leuconostoc mesenteroides has been investigated by a, structural and functional characterization of the D177N mutant enzyme. Its, three-dimensional structure has been determined by X-ray, cryocrystallography in the presence of NAD(+) and in the presence of, glucose 6-phosphate plus NADPH. The structure of a glucose 6-phosphate, complex of a mutant (Q365C) with normal enzyme activity has also been, determined and substrate binding compared. To understand the effect of, Asp-177 on the ionization properties of the catalytic base His-240, the pH, dependence of kinetic parameters has been determined for the D177N mutant, and compared to that of the wild-type enzyme. The structures give details, of ... [(full description)]
About this StructureAbout this Structure
1E77 is a [Single protein] structure of sequence from [Leuconostoc mesenteroides] with BG6 and CA as [ligands]. Active as [[1]], with EC number [1.1.1.49]. Full crystallographic information is available from [OCA].
ReferenceReference
An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme., Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR, Biochemistry. 2000 Dec 12;39(49):15002-11. PMID:11106478
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