Article
Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis.
Biological chemistry - 1 Nov 2009
Urscher Miriam, Deponte Marcel
Abstract excerpt
Glyoxalase II (GloII) is a ubiquitous thioester hydrolase catalyzing the last step of the glutathione-dependent conversion of 2-oxoaldehydes to 2-hydroxycarboxylic acids. Here, we present a detailed structure-function analysis of cGloII from the malaria parasite Plasmodium falciparum. The activity of the enzyme was salt-sensitive and pH-log k(cat) and pH-log k(cat)/K(m) profiles revealed acid-base catalysis. An...
Topics
- Arginine
- Biocatalysis
- Catalytic Domain
- Enzyme Inhibitors
- Glutathione
- Humans
- Hydrogen-Ion Concentration
- Hydroxides
- Kinetics
- Lysine
- Metals
- Models, Molecular
- Mutation
- Plasmodium falciparum
- Salts
- Sequence Alignment
- Structure-Activity Relationship
- Thiolester Hydrolases