Polyneuridine Aldehyde Esterase: Difference between revisions

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Because the cap domain and the architecture of the binding pocket of '''PNAE''' determines its exceptional high substrate specificity, future systematic structure-based, second-sphere, and random mutations should give '''PNAE''' mutants with altered, especially low, substrate specificity. Such enzymes then could be useful multipurpose catalysts for generation of novel alkaloid structures for biological screening.
Because the cap domain and the architecture of the binding pocket of '''PNAE''' determines its exceptional high substrate specificity, future systematic structure-based, second-sphere, and random mutations should give '''PNAE''' mutants with altered, especially low, substrate specificity. Such enzymes then could be useful multipurpose catalysts for generation of novel alkaloid structures for biological screening.
<applet load='3GZJ' size='300' frame='true' align='right' caption='Insert caption here' />
<applet load='3GZJ' size='300' frame='true' align='right' caption='Polyneuridine aldehyde esterase complex with epi-vellosimine [[3gzj]]' />

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Liuqing Yang, Michal Harel, Alexander Berchansky, Joel L. Sussman