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Literature summary extracted from

  • Urscher, M.; Deponte, M.
    Plasmodium falciparum glyoxalase II: Theorell-Chance product inhibition patterns, rate-limiting substrate binding via Arg(257)/Lys(260), and unmasking of acid-base catalysis (2009), Biol. Chem., 390, 1171-1183.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.6 into pQE30 vector. N-terminally MRGS(H)6GS-tagged GloII wild-type and mutant enzymes transformed into Escherichia coli competent XL1-Blue cells or EZ cells Plasmodium falciparum

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.6 K260D unaltered metal binding sites and is correctly folded, but reduced activity. Has a much lower catalytic efficiency, but the spectrum is very similar to the wild-type enzyme. Has a highly simplified bell-shaped pH-activity profile with a maximum at pH 6.7 in contrast to the broad asymmetric profiles of the other enzymes Plasmodium falciparum
3.1.2.6 K260Q unaltered metal binding sites and is correctly folded, but reduced activity Plasmodium falciparum
3.1.2.6 R154K unaltered metal binding sites and is correctly folded, but reduced activity Plasmodium falciparum
3.1.2.6 R154M unaltered metal binding sites and is correctly folded, but reduced activity Plasmodium falciparum
3.1.2.6 R257D unaltered metal binding sites and is correctly folded, but reduced activity Plasmodium falciparum
3.1.2.6 R257Q unaltered metal binding sites and is correctly folded, but reduced activity Plasmodium falciparum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.2.6 D-lactate competitive inhibition Plasmodium falciparum
3.1.2.6 glutathione non-competitive inhibition. Is a stronger inhibitor than the ethyl ester of glutathione. Theorell-Chance Bi Bi mechanism with glutathione as the second product Plasmodium falciparum
3.1.2.6 glutathione ethyl ester carboxylate group of the glycine-moiety is modified, non-competitive inhibition Plasmodium falciparum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.6 0.114
-
 S-D-lactoylglutathione wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 0.116
-
 S-D-lactoylglutathione mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 0.275
-
 S-D-lactoylglutathione mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 2.551
-
 S-D-lactoylglutathione mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4 Plasmodium falciparum
3.1.2.6 2.867
-
 S-D-lactoylglutathione mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 4.308
-
 S-D-lactoylglutathione mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 5.782
-
 S-D-lactoylglutathione mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.2.6 Zinc recombinant GloII is zinc-dependent Plasmodium falciparum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.2.6 31800
-
 x * 31800, His-tagged GloII, SDS-PAGE Plasmodium falciparum

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.6 Plasmodium falciparum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.6 wild-type and glutathione-binding site mutants, by sonication, centrifugation and on Ni-NTA column Plasmodium falciparum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.6 S-D-lactoylglutathione + H2O substrate is predominantly bound via ionic interactions with the conserved residues Arg257 and Lys260. Correct substrate binding is a pH- and salt-dependent rate-limiting step for catalysis. Bi Bi mechanism with the direct involvement of a hydroxide ion as a second substrate Plasmodium falciparum D-lactate + glutathione
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.2.6 ? x * 31800, His-tagged GloII, SDS-PAGE Plasmodium falciparum

Synonyms

EC Number Synonyms Comment Organism
3.1.2.6 GloII
-
 Plasmodium falciparum
3.1.2.6 glyoxalase II
-
 Plasmodium falciparum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.2.6 60
-
 S-D-lactoylglutathione mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 67
-
 S-D-lactoylglutathione mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4 Plasmodium falciparum
3.1.2.6 74
-
 S-D-lactoylglutathione mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 171
-
 S-D-lactoylglutathione mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 222
-
 S-D-lactoylglutathione mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 285
-
 S-D-lactoylglutathione mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 375
-
 S-D-lactoylglutathione wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.1.2.6 0.000031
-
 D-lactate inhibitor binding to the free enzyme, at 25°C, pH 6.8 Plasmodium falciparum
3.1.2.6 3.5
-
 glutathione inhibitor binding to the free enzyme, at 25°C, pH 6.8 Plasmodium falciparum
3.1.2.6 13
-
 glutathione inhibitor binding to the occupied enzyme, at 25°C, pH 6.8 Plasmodium falciparum
3.1.2.6 14
-
 glutathione ethyl ester inhibitor binding to the free enzyme, at 25°C, pH 6.8 Plasmodium falciparum
3.1.2.6 49
-
 glutathione ethyl ester inhibitor binding to the occupied enzyme, at 25°C, pH 6.8 Plasmodium falciparum

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.2.6 11
-
 S-D-lactoylglutathione mutant R257D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 26
-
 S-D-lactoylglutathione mutant K260D, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 30
-
 S-D-lactoylglutathione mutant R257Q, at 25°C, in 100 mM MOPS/NaOH, pH 7.4 Plasmodium falciparum
3.1.2.6 41
-
 S-D-lactoylglutathione mutant K260Q, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 810
-
 S-D-lactoylglutathione mutant R154M, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 2400
-
 S-D-lactoylglutathione mutant R154K, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum
3.1.2.6 3300
-
 S-D-lactoylglutathione wild-type, at 25°C, in 100 mM MOPS/NaOH, pH 6.8 Plasmodium falciparum