A family of highly conserved glycosomal 2-hydroxyacid dehydrogenases from Phytomonas sp.
(2000) Journal of Biological Chemistry — Vol. 275, n° 41, p. 31833-31837 (2000)
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- Abstract
- Phytomonas sp. contains two malate dehydrogenase isoforms, a mitochondrial isoenzyme with a high specificity for oxaloacetate and a glycosomal isozyme that acts on a broad range of substrates (Uttaro, A. D., and Opperdoes, F.R. (1997) Mol. Biochem. Parasitol. 89, 51-59). Here, we show that the low specificity of the latter isoenzyme is the result of a number of recent gene duplications that gave rise to a family of glycosomal 2-hydroxyacid dehydrogenase genes. Two of these genes were cloned, sequenced, and overexpressed in Escherichia coli. Although both gene products have 322 amino acids, share 90.4% identical residues, and have a similar hydrophobicity profile and net charge, their kinetic properties were strikingly different. One isoform behaved as a real malate dehydrogenase with a high specificity for oxaloacetate, whereas the other showed no activity with oxaloacetate but was able to reduce other oxoacids, such as phenyl pyruvate, 2-oxoisocaproate, 2-oxovalerate, 2-oxobutyrate, 2-oxo-4-methiolbutyrate, and pyruvate.
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Uttaro, A. D., Altabe, S. G., Rider, M. H., Michels, P., & Opperdoes, F. (2000). A family of highly conserved glycosomal 2-hydroxyacid dehydrogenases from Phytomonas sp. Journal of Biological Chemistry, 275(41), 31833-31837. https://doi.org/10.1074/jbc.M006080200 (Original work published 2000)