Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion.
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.
Iozef
Rimma
R
Interdisciplinary Research Center, Justus Liebig University, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany.
Rahlfs
Stefan
S
Chang
Tammy
T
Schirmer
Heiner
H
Becker
Katja
K
D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D019143:Evolution, Molecular; D005978:Glutathione / Q000737:chemistry / Q000378:metabolism; D006037:Glyoxal / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D007791:Lactoylglutathione Lyase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010963:Plasmodium falciparum / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000737:chemistry / Q000378:metabolism
D021122:Protein Subunits; D011994:Recombinant Proteins; D006037:Glyoxal; D007791:Lactoylglutathione Lyase; D005978:Glutathione; D015032:Zinc