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Literature summary extracted from

  • Creighton, D.J.; Hamilton, D.S.
    Brief history of glyoxalase I and what we have learned about metal ion-dependent, enzyme-catalyzed isomerizations (2001), Arch. Biochem. Biophys., 387, 1-10.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.5
-
 Escherichia coli
4.4.1.5 crystal structure of glyoxalase I complexed with S-benzylglutathione and S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.5 E172Q 100000fold lower activity than wild-type Homo sapiens
4.4.1.5 E99Q 10000fold lower activity than wild-type Homo sapiens
4.4.1.5 E99Q/Q33E 100fold lower activity than wild-type Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.5 S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
 Homo sapiens
4.4.1.5 S-benzylglutathione
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.5 Co2+ 66% of activity with Zn2+ Homo sapiens
4.4.1.5 Mg2+ 101% of activity with Zn2+ Homo sapiens
4.4.1.5 Mn2+ 67% of activity with Zn2+ Homo sapiens
4.4.1.5 Zn2+ required for activity Homo sapiens
4.4.1.5 Zn2+ required for activity, 1 Zn2+ per subunit Saccharomyces cerevisiae
4.4.1.5 Zn2+ required for activity, no activity with Ni2+, Co2+ and Cd2+ Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.5 glutathione-methylglyoxal hemithioacetal Escherichia coli glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione (R)-S-lactoylglutathione
-
 ?
4.4.1.5 glutathione-methylglyoxal hemithioacetal Saccharomyces cerevisiae glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione (R)-S-lactoylglutathione
-
 ?
4.4.1.5 glutathione-methylglyoxal hemithioacetal Homo sapiens glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate (R)-S-lactoylglutathione
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Escherichia coli
-
-
-
4.4.1.5 Homo sapiens
-
-
-
4.4.1.5 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.5 glutathione-methylglyoxal hemithioacetal glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione Escherichia coli (R)-S-lactoylglutathione
-
 ?
4.4.1.5 glutathione-methylglyoxal hemithioacetal glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione Homo sapiens (R)-S-lactoylglutathione
-
 ?
4.4.1.5 glutathione-methylglyoxal hemithioacetal glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione Saccharomyces cerevisiae (R)-S-lactoylglutathione
-
 ?
4.4.1.5 glutathione-methylglyoxal hemithioacetal glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione, operates in conjunction with glyoxalase II to convert cytotoxic methylglyoxal to nontoxic D-lactate Homo sapiens (R)-S-lactoylglutathione
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.5 GLXI
-
 Homo sapiens
4.4.1.5 glyoxalase I
-
 Escherichia coli
4.4.1.5 glyoxalase I
-
 Homo sapiens
4.4.1.5 glyoxalase I
-
 Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.4.1.5 0.00001
-
 S-(N-p-iodophenyl-N-hydroxycarbamoyl)glutathione
-
 Homo sapiens
4.4.1.5 0.00028
-
 S-benzylglutathione
-
 Homo sapiens