2xf4

Publication Abstract from PubMed

YcbL has been annotated as either a metallo-beta-lactamase or glyoxalase II, both members of the zinc metallo hydrolase superfamily, that contains many enzymes with a diverse range of activities. Here we report crystallographic and biochemical data for Salmonella enterica serovar typhimurium YcbL that establishes it as glyoxalase II which differs in certain structural and functional properties compared to previously known examples. These features include the insertion of an alpha-helix after residue 87 in Ycbl and truncation of the C-terminal domain which leads to the loss of some recognition determinants for the glutathione substrate. In spite of these changes YcbL has robust glyoxalase II activity. A further difference is that the YcbL structure contains only a single bound metal ion rather than the dual site normally observed for glyoxalase IIs. Activity assays in the presence of various metal ions indicate an increase in activity above basal levels in the presence of manganous and ferrous ions. YcbL thus represents a novel member of the glyoxalase II family.

Structural and functional characterization of Salmonella enterica serovar typhimurium YcbL: An unusual type II glyoxalase.,Stamp AL, Owen P, El Omari K, Nichols CE, Lockyer M, Lamb HK, Charles IG, Hawkins AR, Stammers DK Protein Sci. 2010 Jul 28. PMID:20669241^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.