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10.1074/jbc.R114.572990 http://scihub22266oqcxt.onion/10.1074/jbc.R114.572990 C4215207!4215207 !25210039     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25210039 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25210039 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Biol+Chem 2014 ; 289 (44 ): 30229-30236 Nephropedia Template TP {{tp|p=25210039 |t=2014. Enzyme promiscuity: engine of evolutionary innovation |pdf=|usr=}}{{25210039 }} gab.com Text Enzyme promiscuity: engine of evolutionary innovation JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25210039 #FOAvip Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal to the successful acquisition of novel biological functions. Action on multiple substrates (substrate ambiguity) can be harnessed for performance of functions in the cell that supersede catalysis of a single metabolite. These functions include proofreading, scavenging of nutrients, removal of antimetabolites, balancing of metabolite pools, and establishing system redundancy. In this review, we present examples of enzymes that perform these cellular roles by leveraging substrate ambiguity and then present the structural features that support both specificity and ambiguity. We focus on the phosphatases of the haloalkanoate dehalogenase superfamily and the thioesterases of the hotdog fold superfamily. Twit Text FOAVip Enzyme promiscuity: engine of evolutionary innovation ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25210039 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25210039 #FOAvip English Wikipedia <ref>{{Cite pmid|25210039 }}</ref> Enzyme promiscuity: engine of evolutionary innovation #MMPMID25210039 Pandya C ; Farelli JD ; Dunaway-Mariano D ; Allen KN J Biol Chem 2014[Oct]; 289 (44 ): 30229-30236 PMID25210039 show ga Catalytic promiscuity and substrate ambiguity are keys to evolvability, which in turn is pivotal to the successful acquisition of novel biological functions. Action on multiple substrates (substrate ambiguity) can be harnessed for performance of functions in the cell that supersede catalysis of a single metabolite. These functions include proofreading, scavenging of nutrients, removal of antimetabolites, balancing of metabolite pools, and establishing system redundancy. In this review, we present examples of enzymes that perform these cellular roles by leveraging substrate ambiguity and then present the structural features that support both specificity and ambiguity. We focus on the phosphatases of the haloalkanoate dehalogenase superfamily and the thioesterases of the hotdog fold superfamily. |*Evolution, Molecular [MESH] |Animals [MESH] |Biocatalysis [MESH] |Catalytic Domain [MESH] |Enzymes/*chemistry/genetics [MESH] |Humans [MESH] |Models, Molecular [MESH]Enzyme promiscuity: engine of evolutionary innovation (epmc).pdf DeepDyve Pubget Overpricing