D- and L-lactate dehydrogenases during invertebrate evolution |
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Authors: | Melania E Cristescu David J Innes Jonathon H Stillman Teresa J Crease |
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Institution: | (1) Great Lakes Institute for Environmental Research, University of Windsor, 401 Sunset Avenue, N9B 3P4 Windsor, Ontario, Canada;(2) Department of Biology, Memorial University of Newfoundland, St. John's, A1B 3X9 Newfoundland, Canada;(3) San Francisco State University, Romberg Tiburon Center for Environmental Studies, 3152 Paradise Drive, 94920 Tiburon, CA, USA;(4) Department of Integrative Biology, University of Guelph, 488 Gordon Street, N1G 2W1 Guelph, Ontario, Canada |
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Abstract: | Background The L-lactate and D-lactate dehydrogenases, which are involved in the reduction of pyruvate to L(-)-lactate and D(+)-lactate,
belong to evolutionarily unrelated enzyme families. The genes encoding L-LDH have been used as a model for gene duplication
due to the multiple paralogs found in eubacteria, archaebacteria, and eukaryotes. Phylogenetic studies have suggested that
several gene duplication events led to the main isozymes of this gene family in chordates, but little is known about the evolution
of L-Ldh in invertebrates. While most invertebrates preferentially oxidize L-lactic acid, several species of mollusks, a few arthropods
and polychaetes were found to have exclusively D-LDH enzymatic activity. Therefore, it has been suggested that L-LDH and D-LDH
are mutually exclusive. However, recent characterization of putative mammalian D-LDH with significant similarity to yeast
proteins showing D-LDH activity suggests that at least mammals have the two naturally occurring forms of LDH specific to L-
and D-lactate. This study describes the phylogenetic relationships of invertebrate L-LDH and D-LDH with special emphasis on
crustaceans, and discusses gene duplication events during the evolution of L-Ldh. |
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