Open AccessPrimary stucture of a cytosolic malate dehydrogenase of the amitochondriate eukaryote, Trichomonas vaginalis
Author(s) -
Markoš Anton,
Morris Andrea,
Rozario Catherine,
Müller Miklós
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb07998.x
Subject(s) - trichomonas vaginalis , malate dehydrogenase , eukaryote , cytosol , trichomonas , chemistry , biology , microbiology and biotechnology , biochemistry , enzyme , gene , genome
The nucleotide sequence of a gene coding for a 37 kDa subunit of a cytosolic malate dehydrogenase of Trichomonas vaginalis was established. The sequences of a gDNA clone and a cDNA clone, which lacked seven amino‐terminal codons, were identical, indicating an absence of introns from the gene. Cell fractionation combined with sequencing of peptide fragments of the purified enzyme showed that the gene codes for an expressed cytosolic enzyme. The derived amino acid sequence was closely related to cytosolic malate dehydrogenases from animals and plants and from the eubacteria Thermus aquaticus and Mycobacterium leprae and was more distant from the enzyme of mitochondria and from Escherichia coli and certain other eubacteria. In phylogenetic reconstructions this enzyme shared a most recent common ancestor with other cytosolic enzymes.