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Literature summary extracted from

  • Su, Z.; Sukdeo, N.; Honek, J.F.
    15N-1H HSQC NMR evidence for distinct specificity of two active sites in Escherichia coli glyoxalase I (2008), Biochemistry, 47, 13232-13241.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.5 overexpressed in Escherichia coli BL21 (DE3), purified Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.5 the homodimeric GlxI of Escherichia coli consists of two identical polypeptide chains with one tryptophan on each chain on position 61, with two symmetrical active sites wehre one metal ion has been observed in each individual active site. One active site binds to the Ni2+ ion, and the other active site is observed to be more selelective for a potent inhibitor Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.5 H74Q the native His74 metal ligand substituted with a Gln residue, maintains a homodimeric quaternary structure in solution as does the wild-type enzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.4.1.5 Co2+ GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies Escherichia coli
4.4.1.5 Ni2+ GlxI is a Ni2+/Co2+-activated homodimeric protein containing two symmetric, and dually metallated active sites as characterized by X-ray studies Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Escherichia coli P0AC81
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.5 wild-type and rebombinant protein Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
4.4.1.5 (R)-S-lactoylglutathione = glutathione + 2-oxopropanal methylglyoxal and glutathione form an intermediate, the hemithioacetal, which is catalyzed to S-D-lactoylglutathione by GlxI. Subsequently S-D-lactoylglutathione is hydrolyzed to D-lactate and glutathione by GlxII (EC 3.1.2.6) Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.5 methylglyoxal + glutathione methylglyoxal and glutathione form an intermediate, the hemithioacetal, which is catalyzed to S-D-lactoylglutathione by GlxI. Subsequently S-D-lactoylglutathione is hydrolyzed to D-lactate and glutathione by GlxII (EC 3.1.2.6) Escherichia coli S-((R)-lactoyl)glutathione
-
 ?

Subunits

EC Number Subunits Comment Organism
4.4.1.5 homodimer the homodimeric GlxI of Escherichia coli consists of two identical polypeptide chains with one tryptophan on each chain on position 61, with two symmetrical active sites where one metal ion has been observed in each individual active site. One active site binds to the Ni2+ ion, and the other active site is observed to be more selelective for a potent inhibitor Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.4.1.5 GLXI
-
 Escherichia coli
4.4.1.5 glyoxalase I
-
 Escherichia coli