Convergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase

被引：75

作者：

Wu, G ^{[1
]}

Fiser, A ^{[1
]}

ter Kuile, B ^{[1
]}

Sali, A ^{[1
]}

Müller, M ^{[1
]}

机构：

[1] Rockefeller Univ, New York, NY 10021 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1999年 / 96卷 / 11期

关键词：

D O I：

10.1073/pnas.96.11.6285

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Lactate dehydrogenase (LDH) is present in the amitochondriate parasitic protist Trichomonas vaginalis and some but not ail other trichomonad species. The derived amino acid sequence of T. vaginalis LDH (TvLDH) was found to be more closely related to the cytosolic malate dehydrogenase (MDH) of the same species than to any other LDH. A key difference between the two T. vaginalis sequences was that Arg91 of MDH, known to be important in coordinating the C-4 carboxyl of oxalacetate/malate, was replaced by Leu91 in LDH. The change Leu91Arg by site-directed mutagenesis converted TvLDH into an MDH. The reverse single amino acid change Arg91Leu in TvMDH, however, gave a product with no measurable LDH activity. Phylogenetic reconstructions indicate that TvLDH arose from an MDH relatively recently.

引用

页码：6285 / 6290

页数：6

共 42 条

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