Institute of Biomedical Technology, University of Tampere and Tampere University Hospital, Tampere, Finland.
Bioorg Med Chem. 2013 Mar 15;21(6):1516-21. doi: 10.1016/j.bmc.2012.08.046. Epub 2012 Aug 31.
Carbonic anhydrases (CAs) are essential and ubiquitous enzymes. Thus far, there are no articles on characterization of Drosophila melanogaster α-CAs. Data from invertebrate CA studies may provide opportunities for anti-parasitic drug development because α-CAs are found in many parasite or parasite vector invertebrates. We have expressed and purified D. melanogaster CAH1 and CAH2 as proteins of molecular weights 30kDa and 28kDa. CAH1 is cytoplasmic whereas CAH2 is a membrane-attached protein. Both are highly active enzymes for the CO2 hydration reaction, being efficiently inhibited by acetazolamide. CAH2 in the eye of D. melanogaster may provide a new animal model for CA-related eye diseases. A series of dithiocarbamates were also screened as inhibitors of these enzymes, with some representatives showing inhibition in the low nanomolar range.
碳酸酐酶（CA）是一种必需且普遍存在的酶。到目前为止，还没有关于黑腹果蝇α-CA 特征描述的文章。来自无脊椎动物 CA 研究的数据可能为抗寄生虫药物的开发提供机会，因为α-CAs 存在于许多寄生虫或寄生虫载体无脊椎动物中。我们已经表达和纯化了果蝇 CAH1 和 CAH2 作为分子量为 30kDa 和 28kDa 的蛋白质。CAH1 是细胞质的，而 CAH2 是一种膜结合蛋白。这两种酶都是 CO2 水合反应的高效酶，被乙酰唑胺有效抑制。黑腹果蝇眼睛中的 CAH2 可能为与 CA 相关的眼部疾病提供新的动物模型。一系列二硫代氨基甲酸盐也被筛选为这些酶的抑制剂，其中一些代表物在纳摩尔范围内显示出抑制作用。
