Sánchez L B, Hashimoto T, Müller M
Rockefeller University, New York, NY 10021, USA.
Mol Biochem Parasitol. 1996 Nov 25;82(2):145-51. doi: 10.1016/0166-6851(96)02728-4.
The nucleotide sequence and predicted amino acid sequence of malate dehydrogenase (decarboxylating) or malic enzyme (EC 1.1.1.40) of the amitochondriate protist Giardia lamblia were determined. The overall amino acid identity with malic enzyme sequences from other eukaryotes was between 34 and 39%. Functional domains previously defined in other malic enzymes, the malate-, the ADP- and the NAD(P)-binding domains, were present also in the G. lamblia sequence. In phylogenetic reconstructions, the G. lamblia sequence is part of the eukaryotic clade, but its relative position versus the other early branches of the eukaryotic tree (Trichomonas vaginalis hydrogenosome and plant mitochondria) cannot be firmly established. The results indicate, however, a long, independent evolutionary past of this enzyme.
测定了无线粒体原生生物蓝氏贾第鞭毛虫苹果酸脱氢酶(脱羧)或苹果酸酶(EC 1.1.1.40)的核苷酸序列和预测的氨基酸序列。与其他真核生物的苹果酸酶序列的总体氨基酸同一性在34%至39%之间。先前在其他苹果酸酶中定义的功能结构域,即苹果酸结合结构域、ADP结合结构域和NAD(P)结合结构域,也存在于蓝氏贾第鞭毛虫序列中。在系统发育重建中,蓝氏贾第鞭毛虫序列是真核进化枝的一部分,但其相对于真核树其他早期分支(阴道毛滴虫氢化酶体和植物线粒体)的相对位置尚不能确定。然而,结果表明该酶有着漫长的独立进化历程。