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hsG6PD-G6P (deletion variant, N-terminal 25 residues), substrate binding site hsG6PD-G6P in a complex with G6P shown in the substrate binding site, conserved residues between hsG6PD and lmG6PD form the catalytic dyad necessary for catalysis Kotaka, M., Gover, S., Vandeputte-Rutten, L.,
Au, S.W.N., Lam, V.M.S., Adams, M.J., Structural studies of
glucose-6-phosphate and NADP+ binding to human
glucose-6-phosphate dehydrogenase. (2005) Acta
Crystallogr.,Sect.D 61: 495 2BHL (PDB)
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lmG6PD-G6P (Q365C) mutant variant, substrate binding site lmG6PD-G6P in a complex with G6P shown in the substrate binding site, conserved residues between hsG6PD and lmG6PD form the catalytic dyad necessary for catalysis Cosgrove, M.S., Gover, S., Naylor, C.E., Vandeputte-Rutten, L., Adams, M.J., Levy, H.R., An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphatedehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme. (2000) Biochemistry 39: 15002 (PubMed) 1E77 (PDB) |