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Literature summary for 4.4.1.5 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.
    View publication on PubMed

Application

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(Commentary)

Cloned (Comment) Organism
pQE30 constructs of the wild-type and mutants expressed in Escherichia coli strain M15 Plasmodium falciparum

Protein Variants

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

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

Organism UniProt Comment Textmining
Plasmodium falciparum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by gel filtration Plasmodium falciparum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + methylglyoxal
-
Plasmodium falciparum S-D-lactoylglutathione
-
?

Subunits

Subunits Comment Organism
monomer gel filtration Plasmodium falciparum

Synonyms

Synonyms Comment Organism
GloI
-
Plasmodium falciparum
glyoxalase I
-
Plasmodium falciparum

pH Optimum

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