期刊
AMINO ACIDS
卷 36, 期 1, 页码 99-106出版社
SPRINGER WIEN
DOI: 10.1007/s00726-008-0037-6
关键词
Indoleamine 2,3-dioxygenase; Human; Murine; Thermal stability; pH stability; Kinetics; Inhibiton; Secondary structure
资金
- Australian Research Council
- Sir Zelman Cowen Universities Fund
The hemoprotein indoleamine 2,3-dioxygenase (IDO) is the first and rate-limiting enzyme in the most significant pathway for mammalian tryptophan metabolism. It has received considerable attention in recent years, particularly due to its dual role in immunity and the pathogenesis of many diseases. Reported here are differences and similarities between biochemical behaviour and structural features of recombinant human IDO and recombinant mouse IDO. Significant differences were observed in the conversion of substrates and pH stability. Differences in inhibitor potency and thermal stability were also noted. Secondary structural features were broadly similar but variation between species was apparent, particularly in the alpha-helix portion of the enzymes. With mouse models substituting for human diseases, the differences between mouse and human IDO must be recognised before applying experimental findings from one system to the next.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据