| 書目名稱 | Fortschritte der Chemie organischer Naturstoffe / Progress in the Chemistry of Organic Natural Produ |
| 編輯 | D. R. Adams,M. Brochwicz-Lewinski,A. R. Butler,W. |
| 視頻video | http://file.papertrans.cn/347/346477/346477.mp4 |
| 叢書名稱 | Fortschritte der Chemie organischer Naturstoffe‘ Progress in the Chemistry of Organic Natural Produc |
| 圖書封面 |  |
| 描述 | In order to make further progress in elucidating the mechanism of NOS catalysis it will be essential to throw light on the interaction between the enzyme and its substrate. An understanding of the catalytic site will also assist the development of therapeutically important NOS inhibitors. In particular. it will be useful to uncover any differences that exist between the substrate binding sites of the three NOS isozymes which might be exploited for the development of isoform selective NOS inhibitors. A comparison of NOS to other Arg-binding proteins has shown no significant sequence homology (159). Moreover, the lack of a 3D structure and absence of significant sequence homology between the NOS oxygenase domain and known cytochromes P450 has made it difficult to identify residues and construct a model of the distal heme pocket responsible for substrate binding. However, a number of groups are currently working towards crystallisation of the separate NOS reductase and oxygenase domains of the three isoforms for X-ray diffraction studies; the first X-ray structure is likely to be forthcoming within a matter of months. * The results of these studies are expected to resolve many of the |
| 出版日期 | Book 1999 |
| 關(guān)鍵詞 | NO activity; NO release; Nitric oxide; Stickoxid; biochemistry; chemistry; natural product; polymer |
| 版次 | 1 |
| doi | https://doi.org/10.1007/978-3-7091-6351-1 |
| isbn_softcover | 978-3-7091-7305-3 |
| isbn_ebook | 978-3-7091-6351-1Series ISSN 0071-7886 |
| issn_series | 0071-7886 |
| copyright | Springer-Verlag Wien 1999 |
|Archiver|手機(jī)版|小黑屋|
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