| Item type |
文献 / Documents(1) |
| 公開日 |
2024-03-05 |
| アクセス権 |
|
|
アクセス権 |
open access |
| 資源タイプ |
|
|
資源タイプ識別子 |
http://purl.org/coar/resource_type/c_6501 |
|
資源タイプ |
journal article |
| 出版社版DOI |
|
|
|
識別子タイプ |
DOI |
|
|
関連識別子 |
https://doi.org/10.1016/j.ijbiomac.2023.126070 |
|
|
言語 |
ja |
|
|
関連名称 |
10.1016/j.ijbiomac.2023.126070 |
| 出版タイプ |
|
|
出版タイプ |
AM |
|
出版タイプResource |
http://purl.org/coar/version/c_ab4af688f83e57aa |
| タイトル |
|
|
タイトル |
First crystal structure of an NADP+-dependent l-arginine dehydrogenase belonging to the μ-crystallin family |
|
言語 |
en |
| 著者 |
川上, 竜巳
タカミ, ナオキ
林, 順司
ヨネダ, カズナリ
オオモリ, タケト
大島, 敏久
櫻庭, 春彦
|
| 抄録 |
|
|
内容記述タイプ |
Abstract |
|
内容記述 |
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. |
|
言語 |
en |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
L-Arginine dehydrogenase |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
μ-Crystallin/ornithine cyclodeaminase family |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Crystal structure |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Amino acid dehydrogenase |
| キーワード |
|
|
言語 |
en |
|
主題Scheme |
Other |
|
主題 |
Site-directed mutagenesis |
| 書誌情報 |
en : International Journal of Biological Macromolecules
巻 249,
p. 126070,
発行日 2023-07-29
|
| 収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
01418130 |
| 収録物ID |
|
|
収録物識別子タイプ |
ISSN |
|
収録物識別子 |
18790003 |
| 収録物ID |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA00233999 |
| 収録物ID |
|
|
収録物識別子タイプ |
NCID |
|
収録物識別子 |
AA1153092X |
| 出版者 |
|
|
出版者 |
Elsevier |
|
言語 |
en |
| 権利情報 |
|
|
言語 |
en |
|
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/ |
| EID |
|
|
識別子 |
405134 |
|
識別子タイプ |
URI |
| 言語 |
|
|
言語 |
eng |
ijbiomac_249_126070.pdf (1.38 MB)
