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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Dimerization
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Evolution, Molecular
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Glutathione / chemistry
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Glutathione / metabolism
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Glyoxal / chemistry
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Glyoxal / metabolism
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Humans
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Kinetics
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Lactoylglutathione Lyase / chemistry*
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Lactoylglutathione Lyase / genetics*
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Lactoylglutathione Lyase / metabolism
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Molecular Sequence Data
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Molecular Weight
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Plasmodium falciparum / enzymology*
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Protein Structure, Tertiary
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Protein Subunits
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Sequence Homology, Amino Acid
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Zinc / chemistry
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Zinc / metabolism
Substances
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Protein Subunits
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Recombinant Proteins
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Glyoxal
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Lactoylglutathione Lyase
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Glutathione
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Zinc