@article{open1561,
          volume = {188},
          number = {1},
           month = {October},
          author = {Gurmeet Kaur and Srikrishna Subramanian},
           title = {Repurposing TRASH: emergence of the enzyme organomercurial lyase from a non-catalytic zinc finger scaffold.},
       publisher = {Elsevier},
            year = {2014},
         journal = {Journal of structural biology},
           pages = {16--21},
        keywords = {Domain duplication; Domain fusion; Enzyme evolution; MerA; MerH; NosL; Promiscuous enzymes},
             url = {http://crdd.osdd.net/open/1561/},
        abstract = {The mercury resistance pathway enzyme organomercurial lyase (MerB) catalyzes the conversion of organomercurials to ionic mercury (Hg(2+)). Here, we provide evidence for the emergence of this enzyme from a TRASH-like, non-enzymatic, treble-clef zinc finger ancestor by domain duplication and fusion. Surprisingly, the structure-stabilizing metal-binding core of the treble-clef appears to have been repurposed in evolution to serve a catalytic role. Novel enzymatic functions are believed to have evolved from ancestral generalist catalytic scaffolds or from already specialized enzymes with catalytic promiscuity. The emergence of MerB from a zinc finger ancestor serves as a rare example of how a novel enzyme may emerge from a non-catalytic scaffold with a related binding function.}
}