Application | Comment | Organism |
---|---|---|
additional information | GloI has two functional active sites with similar catalytic activities and pH profiles but different substrate affinities. Glu91/Glu272 and Glu345/Glu161 are isofunctional to Glu99 and Glu172 in human GloI, respectively. As a consequence, Glu91 and Glu345 are part of active site A between the N- and C-terminal domains, and Glu272 and Glu161 form active site B between the intermediate domains. Both active sites are able to adopt two different conformations and are allosterically coupled | Plasmodium falciparum |
Cloned (Comment) | Organism |
---|---|
pQE30 constructs of the wild-type and mutants expressed in Escherichia coli strain M15 | Plasmodium falciparum |
Protein Variants | Comment | Organism |
---|---|---|
E161Q | maximum catalytic efficiency is 60% of the wild-type enzyme | Plasmodium falciparum |
E161Q/E272Q | maximum catalytic efficiency is 60% of the wild-type enzyme | Plasmodium falciparum |
E161Q/E345Q | almost completely inactivated | Plasmodium falciparum |
E161Q/R186/E272Q | kinetics are biphasic | Plasmodium falciparum |
E272Q | maximum catalytic efficiency is 60% of the wild-type enzyme | Plasmodium falciparum |
E345Q | kinetics are biphasic, maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5 | Plasmodium falciparum |
E91Q | maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5 | Plasmodium falciparum |
E91Q/E345Q | maximum catalytic efficiency is 7% of the wild-type enzyme | Plasmodium falciparum |
R22E | decreased substrate affinity | Plasmodium falciparum |
R22E/E91Q/E345Q | kinetics are monophasic, substrate binding at the high-affinity binding site A is abrogated, the mutant seems to be trapped in the conformation that predominates at lower substrate concentrations | Plasmodium falciparum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
S-hexylglutathione | slows degradation of the wild-type enzyme and mutant E161Q/E345Q in comparison with uncomplexed protein | Plasmodium falciparum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Plasmodium falciparum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
by gel filtration | Plasmodium falciparum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
glutathione + methylglyoxal | - |
Plasmodium falciparum | S-D-lactoylglutathione | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | gel filtration | Plasmodium falciparum |
Synonyms | Comment | Organism |
---|---|---|
GloI | - |
Plasmodium falciparum |
glyoxalase I | - |
Plasmodium falciparum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
has a very broad pH optimum with two small local maxima at pH 7.0 and 7.5 and a third local maximum at pH 5.8 | Plasmodium falciparum |