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《CIESC Journal》 2019-01
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Exploring the key structural properties affecting the function of multi-step phytoene dehydrogenase CrtI

CHEN Chen;WANG Ying;LIU Hong;CHEN Yan;YAO Mingdong;XIAO Wenhai;Key Laboratory of Systems Bioengineering, Ministry of Education,Tianjin;SynBio Research Platform,Collaborative Innovation Center of Chemical Science and Engineering,Tianjin;  
A kind of universal enzyme that catalyzes a multi-step continuous reaction in an organism plays an important role in the biological metabolic process. As a typical representative, phytoene dehydrogenase(CrtI) can catalyze multi-step continuous dehydrogenation to produce products of great value such as lycopene. Herein, thecatalytic function of CrtI was studied in Saccharomyces cerevisiae. Firstly, by combining design and screening ofthree heterologous enzymes CrtE, CrtB and CrtI in the lycopene synthesis pathway, CrtI was confirmed as the mainlimiting factor, and CrtI from Blakeslea trispora exerted excellent catalytic function. Through bioinformatics andprotein structural analysis the key residue S311 of BtCrtI was explored, which linked and maintained the keysecondary structure of active center domain. Subsequently, the results of saturation mutation showed that the type ofamino acid residue mutated at S311 had a significant effect on the structure and function of the active centerdomain. This provided a novel structural point for the design and modification of enzymes. Meanwhile, anotherinteresting finding is that the various activity of CrtI mutants did not disturbing the carotenoid metabolic flow in our biosynthesis pathway. Therefore, CrtI is crucial to improve the yield and purity of lycopene.
【Fund】: 国家自然科学基金青年项目(31600052)
【CateGory Index】: O629.8
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