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Literature summary for 4.4.1.5 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
Search for more literature for 4.4.1.5

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Metals/Ions Comment Organism Structure
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
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

Organism UniProt Comment Textmining
Escherichia coli P0AC81
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
(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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Subunits Comment Organism
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

Synonyms Comment Organism
GLXI
-
 Escherichia coli
glyoxalase I
-
 Escherichia coli