@article{oai:nagoya.repo.nii.ac.jp:00030642,
 author = {Ashida, Tamaichi and Yamane, Takashi and Suzuki, Atsuo},
 issue = {1},
 journal = {Memoirs of the School of Engineering, Nagoya University},
 month = {Oct},
 note = {The X-ray crystallographic studies of the structures and functions of several hydrolases and proteinase inhibitor proteins have been carried out. Among Bowman-Birk type inhibitors the crystal of A-II from peanut, the (1:1) complex crystal between trypsin and AB-I from adzuki bean, and the (1:2) complex crystal of the same type inhibitor I-2 from wheat germ with trypsin have been studied at 2.3Å resolution, and the inhibition mechanism as well as the molecular structure of the BBI inhibitors were made clear. The structure of  phospholipase A2 from venom of  habu snake (Trimeresurus flavoviridis) was studied at  the 1.5Å resolution, and the precise molecular structure, including the structures of catalytic triad, Asp-His-H[2]O, the "Ca-binding site", and several important water molecules for the activity of the enzyme were discussed. The effect of pH for the molecular structure of the enzyme was discussed with respect to its activity. The structures of other enzymes such as, an alkaline proteinase of subtilisin type from Bacillus sp. KSM-K16, trypsin of Streptomyces erythraeus, and thermostable bacterial α-amylase were also studied.},
 pages = {1--45},
 title = {Crystallographic structural study of some hydrolases (hydrolytic enzymes) and their inhibitor proteins},
 volume = {47},
 year = {1995}
}