直近一年間の累計
アクセス数 : ?
ダウンロード数 : ?
ID 119010
著者
Takami, Naoki Kagawa University
Yoneda, Kazunari Tokai University
Ohmori, Taketo Osaka Institute of Technology
櫻庭, 春彦 Kagawa University
キーワード
L-Arginine dehydrogenase
μ-Crystallin/ornithine cyclodeaminase family
Crystal structure
Amino acid dehydrogenase
Site-directed mutagenesis
資料タイプ
学術雑誌論文
抄録
Crystal structures of Pseudomonas veronii L-arginine dehydrogenase (L-ArgDH), belonging to the μ-crystallin/ornithine cyclodeaminase family, were determined for the enzyme in complex with L-lysine and NADP+ and with L-arginine and NADPH. The main chain coordinates of the P. veronii L-ArgDH monomer showed notable similarity to those of Archaeoglobus fulgidus L-AlaDH, belonging to the same family, and pro-R specificity similar to L-AlaDH for hydride transfer to NADP+ was postulated. However, the residues recognizing the α-amino group of the substrates differed between the two enzymes. Based on a substrate modeling study, it was proposed that in A. fulgidus L-AlaDH, the amino group of L-alanine interacts via a water molecule (W510) with the side chains of Lys41 and Arg52. By contrast, the α-amino group of L-arginine formed hydrogen bonds with the side chains of Thr224 and Asn225 in P. veronii L-ArgDH. Moreover, the guanidino group of L-arginine was fixed into the active site via hydrogen bonds with the side chain of Asp54. Site-directed mutagenesis suggested that Asp54 plays an important role in maintaining high reactivity against the substrate and that Tyr58 and Lys71 play critical roles in enzyme catalysis.
掲載誌名
International Journal of Biological Macromolecules
ISSN
01418130
18790003
cat書誌ID
AA00233999
AA1153092X
出版者
Elsevier
249
開始ページ
126070
発行日
2023-07-29
権利情報
© 2023. This manuscript version is made available under the CC-BY-NC-ND 4.0 license https://creativecommons.org/licenses/by-nc-nd/4.0/
EDB ID
出版社版DOI
出版社版URL
フルテキストファイル
言語
eng
著者版フラグ
著者版
部局
生物資源系