Glyoxalase I (4.4.1.5) (lactoylglutathione lyase) catalyzes the first step of the glyoxal pathway. S-lactoylglutathione is then converted by glyoxalase II to lactic acid [1].Glyoxalase I is an ubiquitous enzyme which binds one mole of zincper subunit. The bacterial and yeast enzymes are monomeric while the mammalian one is homodimeric. The sequence of glyoxalase I is well conserved.

The domain represented by this entry is found in glyoxalase I and in other related proteins, including fosfomycin resistance proteins FosB [2], FosA [3], FosX [4] and dioxygenases (eg. 4-hydroxyphenylpyruvate dioxygenase).

1. Human glyoxalase I. cDNA cloning, expression, and sequence similarity to glyoxalase I from Pseudomonas putida. J. Biol. Chem. 268, 11217-21
2. FosB, a cysteine-dependent fosfomycin resistance protein under the control of sigma(W), an extracytoplasmic-function sigma factor in Bacillus subtilis. J. Bacteriol. 183, 2380-3
3. Functional analysis of active site residues of the fosfomycin resistance enzyme FosA from Pseudomonas aeruginosa. J. Biol. Chem. 280, 17786-91
4. Structure and mechanism of the genomically encoded fosfomycin resistance protein, FosX, from Listeria monocytogenes. Biochemistry 46, 8110-20

Glyoxalase I (Show more...

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