Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

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.
    View publication on PubMed

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