Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: An unusual Type II glyoxalase
作者： Anna L. Stamp , Paul Owen , Kamel El Omari , Charles E. Nichols , Michael Lockyer
DOI: 10.1002/PRO.475
关键词:
摘要: YcbL has been annotated as either a metallo-β-lactamase or glyoxalase II (GLX2), both members of the zinc metallohydrolase superfamily, that contains many enzymes with diverse range activities. Here, we report crystallographic and biochemical data for Salmonella enterica serovar Typhimurium establishes it GLX2, which differs in certain structural functional properties compared previously known examples. These features include insertion an α-helix after residue 87 truncation C-terminal domain, leads to loss some recognition determinants glutathione substrate. Despite these changes, robust GLX2 activity. A further difference is structure only single bound metal ion rather than dual site normally observed GLX2s. Activity assays presence various ions indicate increase activity above basal levels manganous ferrous ions. Thus, represents novel member family.
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