S
IPR018146

Glyoxalase I, conserved site

InterPro entry
Short nameGlyoxalase_1_CS

Description

Glyoxalase I (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway in the following reaction:

glutathione + methylglyoxal = (R)-S-lactoylglutathione

S-lactoylglutathione is then converted by glyoxalase II to lactic acid
[1]
. Glyoxalase I is a ubiquitous enzyme which binds one mole of zinc per subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved. In bacteria and mammals the enzyme is a protein of about 130 to 180 residues while in fungi it is about twice as long. In these organisms the enzyme is built out of the tandem repeat of a homologous domain.

References

1.Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. Kim NS, Umezawa Y, Ohmura S, Kato S. J. Biol. Chem. 268, 11217-21, (1993). View articlePMID: 7684374

GO terms

biological process

  • None

cellular component

  • None

Cross References

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