Dalrymple B P, Peters J M, Vuocolo T
Commonwealth Scientific and Industrial Research Organisation, Division of Tropical Animal Production, Indooroopilly, Queensland, Australia.
Biochem Int. 1992 Dec;28(4):651-7.
The predicted amino acid sequence of the protein encoded by a cDNA clone isolated from the protozoan haemoparasite Babesia bovis has approximately 22% amino acid identity with the Pichia stipitis xylose reductase. There are similar levels of amino acid identity with other members of the aldo-keto reductase superfamily. The identities include many residues highly conserved in the superfamily. However, the amino acid sequence of the B. bovis protein (AKR1) clearly lies outside the cluster of the previously characterized members of the superfamily. A putative protein encoded by a previously undescribed partially characterized open reading frame at the igrA (increased glyphosate resistance) locus of Pseudomonas sp. strain PG2982 also exhibits similarity to AKR1 and the aldo-keto reductases.
从原生动物血液寄生虫牛巴贝斯虫分离出的一个cDNA克隆所编码蛋白质的预测氨基酸序列，与树干毕赤酵母木糖还原酶具有约22%的氨基酸同一性。与醛酮还原酶超家族的其他成员也有相似水平的氨基酸同一性。这些同一性包括超家族中许多高度保守的残基。然而，牛巴贝斯虫蛋白质（AKR1）的氨基酸序列显然位于该超家族先前已鉴定成员的聚类之外。假单胞菌属PG2982菌株igrA（草甘膦抗性增强）位点处一个先前未描述且部分特征化的开放阅读框所编码的推定蛋白质，也与AKR1和醛酮还原酶表现出相似性。
