Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion |
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Authors: | Iozef Rimma Rahlfs Stefan Chang Tammy Schirmer Heiner Becker Katja |
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Affiliation: | Interdisciplinary Research Center, Justus Liebig University, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany. |
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Abstract: | Recombinant Plasmodium falciparum glyoxalase I (PfGlx I) was characterized as monomeric Zn(2+)-containing enzyme of 44 kDa. The K(M) value of the methylglyoxal-glutathione adduct is 77+/-15 microM, the k(cat) value being 4000 min(-1) at 25 degrees C and pH 7.0. PfGlx I consists of two halves, each of which is homologous to the small 2-domain glyoxalase I of man. Both parts of the pfglx I gene were overexpressed; the C-terminal half of PfGlx I was found to be a stable protein and formed an enzymatically active dimer. These results support the hypothesis of domain-swapping and subunit fusion as mechanisms in glyoxalase I evolution. |
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Keywords: | Glutathione Glyoxalase Malaria Methylglyoxal Plasmodium falciparum |
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