2007年
New insights into the binding mode of coenzymes: Structure of Thermus thermophilus Δ1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
- ,
- ,
- ,
- ,
- ,
- ,
- 巻
- 63
- 号
- 6
- 開始ページ
- 462
- 終了ページ
- 465
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1107/S1744309107021422
- 出版者・発行元
- BLACKWELL PUBLISHING
Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDh) is known to preferentially use NAD+ as a coenzyme. The k(cat) value of Thermus thermophilus P5CDh (TtP5CDh) is four times lower for NADP(+) than for NAD(+). The crystal structure of NADP(+)-bound TtP5CDh was solved in order to study the structure-activity relationships for the coenzymes. The binding mode of NADP(+) is essentially identical to that in the previously solved NAD(+)-bound form, except for the regions around the additional 2 '-phosphate group of NADP(+). The coenzyme-binding site can only accommodate this group by the rotation of a glutamate residue and subtle shifts in the main chain. The 2 '-phosphate of NADP(+) increases the number of hydrogen bonds between TtP5CDh and NADP(+) compared with that between TtP5CDh and NAD(+). Furthermore, the phosphate of the bound NADP(+) would restrict the 'bending' of the coenzyme because of steric hindrance. Such bending is important for dissociation of the coenzymes. These results provide a plausible explanation of the lower turnover rate of NADP(+) compared with NAD(+).
- リンク情報
-
- DOI
- https://doi.org/10.1107/S1744309107021422
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000248045100002&DestApp=WOS_CPL
- URL
- http://www.scopus.com/inward/record.url?eid=2-s2.0-34249946589&partnerID=MN8TOARS
- ID情報
-
- DOI : 10.1107/S1744309107021422
- ISSN : 1744-3091
- ORCIDのPut Code : 58433934
- SCOPUS ID : 34249946589
- Web of Science ID : WOS:000248045100002