精氨酸酶
鸟氨酸
计算生物学
精氨酸
化学
药理学
生物化学
医学
生物
氨基酸
作者
Jason Muller,Rym Attia,Andy Zedet,Christian Girard,Marc Pudlo
出处
期刊:Mini-reviews in Medicinal Chemistry
[Bentham Science]
日期:2022-08-01
卷期号:22 (15): 1963-1976
标识
DOI:10.2174/1389557522666211229105703
摘要
Arginase, which converts arginine into ornithine and urea, is a promising therapeutic target. Arginase is involved in cardiovascular diseases, parasitic infections and through a critical role in immunity, in some cancers. There is a need to develop effective arginase inhibitors and therefore efforts to identify and optimize new inhibitors are increasing. Several methods of evaluating arginase activity are available, but few directly measure the product. Radiometric assays need to separate urea and dying reactions require acidic conditions and sometimes heating. Hence, there are a variety of different approaches available, and each approach has its own limits and benefits. In this review, we provide an update on arginase inhibitors, followed by a discussion on available arginase assays and alternative methods, focusing on the intrinsic biases and parameters that are likely to impact results.
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