Structures of almond hydroxynitrile lyase isoenzyme 5 provide a rationale for the lack of oxidoreductase activity in flavin dependent HNLs
详细信息 查看全文
- 作者：Tea Pavkov-Kellera ; b ; Janny Bakhuisc ; Georg Steinkellnera ; b ; Fenneke Jolinkc ; Esther Keijmelc ; Ruth Birner-Gruenbergera ; d ; Karl Grubera ; b ; karl.gruber@uni-graz.at" class="auth_mail" title="E-mail the corresponding author
- 关键词：HNL ; hydroxynitrile lyase ; PaHNL ; HNL from Prunus amygdalus ; AAO ; aryl-alcohol oxidase
- 刊名：Journal of Biotechnology
- 出版年：2016
- 出版时间：10 October 2016
- 年：2016
- 卷：235
- 期：Complete
- 页码：24-31
- 全文大小：1504 K
文摘
- class="listitem" id="list_lis0005">
- class="label">•
Structure determination of highly glycosylated PaHNL5 expressed in Aspergillus niger and its complex with benzyl alcohol.
- class="label">•
Comparison with the structure of PaHNL1 reveals a higher accessibility to the active site and a larger cavity for PaHNL5.
- class="label">•
Benzyl alcohol is bound too distant from FAD in order to directly participate in the redox mechanism proposed for AAOs.
© 2004-2018 中国地质图书馆版权所有 京ICP备05064691号 京公网安备11010802017129号 地址：北京市海淀区学院路29号 邮编：100083 电话：办公室：(+86 10)66554848；文献借阅、咨询服务、科技查新：66554700 |