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PROSITE documentation PDOC00720 [for PROSITE entry PS00934]

Glyoxalase I signatures





Description

Glyoxalase I (EC 4.4.1.5) (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway, the transformation of methylglyoxal and glutathione into S-lactoylglutathione which is then converted by glyoxalase II to lactic acid [1]. Glyoxalase I is an 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 longer. In these organisms the enzyme is built out of the tandem repeat of an homologous domain.

We have derived two signature patterns for this family. The first one is located in the N-terminal region while the second one is located in the central section of the protein and contains a conserved histidine that could be implicated in the binding of the zinc atom.

Last update:

December 2004 / Pattern and text revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

GLYOXALASE_I_1, PS00934; Glyoxalase I signature 1  (PATTERN)

GLYOXALASE_I_2, PS00935; Glyoxalase I signature 2  (PATTERN)


Reference

1AuthorsKim N.-S. Umezawa Y. Ohmura S. Kato S.
TitleHuman glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida.
SourceJ. Biol. Chem. 268:11217-11221(1993).
PubMed ID7684374



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