Dalby A, Littlechild J A
Department of Chemistry, University of Exeter, UK.
J Pharm Pharmacol. 1996 Feb;48(2):214-7. doi: 10.1111/j.2042-7158.1996.tb07126.x.
A structural study of the type I aldolases has been carried out to examine the isozyme specificity of these enzymes and the potential for designing specific inhibitors. Natural mutations in these aldolase enzymes are associated with haemolytic anaemia and fructose intolerance. It has also been proposed that inhibition of the parasitic version of the enzyme may provide a new lead in the design of drugs against malaria and sleeping sickness. X-ray crystallographic data is used with molecular modelling techniques to investigate the structural properties of these enzymes.
对I型醛缩酶进行了结构研究，以检验这些酶的同工酶特异性以及设计特异性抑制剂的可能性。这些醛缩酶中的自然突变与溶血性贫血和果糖不耐受有关。也有人提出，抑制该酶的寄生形式可能为设计抗疟疾和昏睡病的药物提供新的线索。利用X射线晶体学数据和分子建模技术来研究这些酶的结构特性。
