Glyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusion

FEBS Letters

Rahlfs, Stefan¹  Chang, Tammy¹  Schirmer, Heiner²  Becker, Katja¹  Iozef, Rimma¹ 

[1] Interdisciplinary Research Center, Justus Liebig University, Heinrich-Buff-Ring 26-32, D-35392 Giessen, Germany;Biochemistry Center, Ruprecht Karls University, D-69120 Heidelberg, Germany

关键词: Glutathione;    Glyoxalase;    Malaria;    Methylglyoxal;    Plasmodium falciparum;   

DOI  :  10.1016/S0014-5793(03)01146-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recombinant Plasmodium falciparum glyoxalase I (PfGlx I) was characterized as monomeric Zn²⁺-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.

【 授权许可】

Unknown