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Convergent evolution of Trichomonas vaginalis lactate dehydrogenase from malate dehydrogenase

By Gang Wu, András Fiser, Benno ter Kuile, Andrej Šali and Miklós Müller

Abstract

Lactate dehydrogenase (LDH) is present in the amitochondriate parasitic protist Trichomonas vaginalis and some but not all 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

Topics: Biological Sciences
Publisher: The National Academy of Sciences
Year: 1999
OAI identifier: oai:pubmedcentral.nih.gov:26873
Provided by: PubMed Central
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