TY  - JOUR
ID  - open1561
UR  - http://www.sciencedirect.com/science/article/pii/S1047847714001877
IS  - 1
A1  - Kaur, Gurmeet
A1  - Subramanian, Srikrishna
Y1  - 2014/10//
N2  - 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.
PB  - Elsevier
JF  - Journal of structural biology
VL  - 188
KW  - Domain duplication; Domain fusion; Enzyme evolution; MerA; MerH; NosL; Promiscuous enzymes
SN  - 1095-8657
TI  - Repurposing TRASH: emergence of the enzyme organomercurial lyase from a non-catalytic zinc finger scaffold.
SP  - 16
EP  - 21
ER  -