@article{oai:tohoku-mpu.repo.nii.ac.jp:00000308,
 author = {小林, 佳奈 and Kobayashi, Kana and 村上, 知之 and Murakami, Tomoyuki and 吉田, 崇志 and Yoshida, Takashi and 小田, 彰史 and Oda, Akifumi and 高橋, 央宜 and Takahashi, Ohgi},
 issue = {58},
 journal = {東北薬科大学研究誌, Journal of Tohoku Pharmaceutical University},
 month = {Dec},
 note = {recently, D-amino acids have been found to exist in the human body both as free amino acids and as residues in proteins. The free D-Asp is degraded by d-aspartate oxidase(DDO). DDO with cofactor FAD catalyzes the oxidative deamination of D-Asp and oxaloacetic acid is generated. On the other hand, it is reported that DDO with cofactor FADH2 can also form a complex with D-Asp. in this study, computational docking between D-Asp and DDO was carried out with FAD or FADH2 as the cofactor. The results of docking studies indicate that D-Asp can be recognized both by DDO with FAD and DDO with FADH2, and the difference in binding affinity between the oxidative and reductive states is caused by difference of hydrogen bonding patterns.},
 pages = {35--40},
 title = {FADおよびFADH2存在下におけるD-アスパラギン酸酸化酵素とD-アスパラギン酸のドッキングシュミレーション},
 year = {2011},
 yomi = {コバヤシ, カナ and ムラカミ, トモユキ and ヨシダ, タカシ and オダ, アキフミ and タカハシ, オウギ}
}