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Glyoxalase I of the malarial parasite Plasmodium falciparum : evidence for subunit fusion
Author(s) -
Iozef Rimma,
Rahlfs Stefan,
Chang Tammy,
Schirmer Heiner,
Becker Katja
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01146-3
Subject(s) - methylglyoxal , plasmodium falciparum , lactoylglutathione lyase , protein subunit , dimer , glutathione , chemistry , biochemistry , recombinant dna , enzyme , fusion protein , biology , microbiology and biotechnology , gene , malaria , organic chemistry , immunology
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 μM, the k cat value being 4000 min −1 at 25°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.