Ramos Marco A, Mares Rosa E, Magaña Paloma D, Ortega Joaquín E, Cornejo-Bravo Jose M
Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico 14418, Tijuana, Baja California, México 22390, Mexico.
Comput Biol Chem. 2008 Feb;32(1):66-70. doi: 10.1016/j.compbiolchem.2007.09.002. Epub 2007 Sep 14.
Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze the correct formation of disulfide bonds during protein folding. Structurally they are characterized by the presence of functional thioredoxin-like (Trx) domains. For the protozoan parasite causative of the human amebiasis (Entamoeba histolytica), the correct formation of disulfide bonds is important for an accurate folding of its proteins, including some virulence factors. However, little is known about the enzymes involved in this mechanism. We undertook a post-genomic approach to identify the PDI family of this parasite. The genome database survey revealed a set of 11 PDI-encoding sequences with predictable protein thiol/disulfide oxidoreductase activities.
蛋白质二硫键异构酶（PDI）是真核生物氧化还原酶，在蛋白质折叠过程中催化二硫键的正确形成。从结构上看，它们的特征是存在功能性硫氧还蛋白样（Trx）结构域。对于引起人类阿米巴病的原生动物寄生虫（溶组织内阿米巴）而言，二硫键的正确形成对于其蛋白质（包括一些毒力因子）的精确折叠很重要。然而，对于参与这一机制的酶了解甚少。我们采用后基因组方法来鉴定该寄生虫的PDI家族。基因组数据库调查揭示了一组11个具有可预测的蛋白质硫醇/二硫键氧化还原酶活性的PDI编码序列。
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