Literature summary extracted from
Deponte, M.; Sturm, N.; Mittler, S.; Harner, M.; Mack, H.; Becker, K.
Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I (2007), J. Biol. Chem., 282, 28419-28430.
Application
EC Number |
Application |
Comment |
Organism |
---|
4.4.1.5 |
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(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.4.1.5 |
pQE30 constructs of the wild-type and mutants expressed in Escherichia coli strain M15 |
Plasmodium falciparum |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.4.1.5 |
E161Q |
maximum catalytic efficiency is 60% of the wild-type enzyme |
Plasmodium falciparum |
4.4.1.5 |
E161Q/E272Q |
maximum catalytic efficiency is 60% of the wild-type enzyme |
Plasmodium falciparum |
4.4.1.5 |
E161Q/E345Q |
almost completely inactivated |
Plasmodium falciparum |
4.4.1.5 |
E161Q/R186/E272Q |
kinetics are biphasic |
Plasmodium falciparum |
4.4.1.5 |
E272Q |
maximum catalytic efficiency is 60% of the wild-type enzyme |
Plasmodium falciparum |
4.4.1.5 |
E345Q |
kinetics are biphasic, maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5 |
Plasmodium falciparum |
4.4.1.5 |
E91Q |
maximum catalytic efficiency is 7% of the wild-type enzyme, sensitive to pH values less than 6.5 |
Plasmodium falciparum |
4.4.1.5 |
E91Q/E345Q |
maximum catalytic efficiency is 7% of the wild-type enzyme |
Plasmodium falciparum |
4.4.1.5 |
R22E |
decreased substrate affinity |
Plasmodium falciparum |
4.4.1.5 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
4.4.1.5 |
S-hexylglutathione |
slows degradation of the wild-type enzyme and mutant E161Q/E345Q in comparison with uncomplexed protein |
Plasmodium falciparum |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.4.1.5 |
Plasmodium falciparum |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.4.1.5 |
by gel filtration |
Plasmodium falciparum |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.4.1.5 |
glutathione + methylglyoxal |
- |
Plasmodium falciparum |
S-D-lactoylglutathione |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
4.4.1.5 |
monomer |
gel filtration |
Plasmodium falciparum |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.4.1.5 |
GloI |
- |
Plasmodium falciparum |
4.4.1.5 |
glyoxalase I |
- |
Plasmodium falciparum |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.4.1.5 |
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 |