| Outline of Final Research Achievements |
We studied on a prostaglandin E synthase (bmPGES) in the silkworm Bombyx mori that involves in the isomerization of PGH2 to PGE2. Also, we identified an aldo-keto reductase 6 (AKR6), new prostaglandin synthase in B. mori. The present study aimed to analyze substrate-binding site in bmPGES and AKR6. Each protein was purified, concentrated to 10 mg/mL in 20mM Tris-HCl, pH8, 0.2M NaCl, and crystallized by sitting-drop vapor diffusion. Results showed we obtained some crystals for both protein, although we were unable to get enough diffraction data. Site-directed mutagenesis experiments revealed that we found amino acid residues regarding to catalysis in bmPGES as well as AKR6. Therefore, this study may provide insights into the physiological role of both proteins in silkworms.
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