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. Author manuscript; available in PMC: 2015 Feb 15.
Published in final edited form as: Arch Biochem Biophys. 2013 Sep 10;0:142–152. doi: 10.1016/j.abb.2013.09.002

Fig. 1.

Fig. 1

Glyoxalase I (GlxI). (A) GlxI acts on the reversibly-formed hemithioacetal product of glutathione (GSH) plus methylglyoxal, and catalyzes formation of S-D-lactoylglutathione via a cis-enediolate intermediate. The product is hydrolyzed by glyoxalase II (GlxII) to yield D-lactate. (B) Glx I structure and active site. The homodimeric protein (cyan and white cartoon view, PDB access code 1f9z, Escherichia coli) contains two Ni-containing active sites (green spheres) at the dimer interface with His and Glu ligands (sticks) contributed by each subunit and two coordinated waters (red spheres).

(2 column width)