Cyclodipeptide synthases (CDPSs) are enzymes that use two aminoacyl-tRNAs as a source of amino acids to catalyze the formation of a class of organic ring structures called 2,5-diketopiperazines (DKPs). DKPs have a rich history of bioactivity and use in drug discovery. DKPs serve as precursors to common pharmaceuticals, such as the oxytocin receptor antagonist Retosiban and the vasodilator Cialis (Tadalafil). CDPSs offer a biochemical and green alternative to what would otherwise be a relatively complex synthetic process. The CDPS gene being characterized currently is SNC-109. SDS-PAGE analysis of protein profiles indicated that the enzymes produced by SNC-109 gene were approximately 25 kDa in size, which corresponded with the theoretical size. To attempt characterization of the molecules whose production is catalyzed by this CDPS, HPLC analysis was conducted on supernatant of <i>E. coli </i>cells transformed with a pQE30-SNC109 vector construct alongside negative controls transformed with empty pQE30 vector only. One major product is preliminarily identified as cyclo (Pro-Tyr). There are approximately 2 other compounds produced that further chemical analysis will aim to identify.

Production and characterization of 2,5-diketopiperazines produced by the cyclodipeptide synthase SNC-109

2019 Spring National Meeting

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