Abstract:
:Carotenoids, a variety of natural products, have significant pharmaceutical and commercial potential. Phytoene dehydrogenase (CrtI) is the rate-limit enzyme for carotenoid synthesis, whose catalysis specificity results in various carotenoids. However, the structural characteristics of CrtI for controlling the catalysis specificity on dehydrogenation steps are still unclear, which limited the development of CrtI function. Here we confirmed two mutation sites H136 and H453 in the mutant library of CrtI from Blakeslea trispora, which markedly regulated catalytic specificity. Interestingly, the sequence alignment features at H136 and H453 were consistent with the phylogenetic analysis of CrtI families. Subsequently, the functions of saturated mutants at H136 and H453 were clustered by principal component analysis (PCA) and k-means. According to the clustering results, diversiform mutants with specific dehydrogenation function provided important application value for carotenoid product customization. Meanwhile, this study also enriched the theory of enzyme evolution and guided the functional development of enzymes.
journal_name
ACS Synth Bioljournal_title
ACS synthetic biologyauthors
Liang N,Chen C,Wang Y,Ding MZ,Yao MD,Xiao WH,Yuan YJdoi
10.1021/acssynbio.0c00128subject
Has Abstractpub_date
2020-07-17 00:00:00pages
1753-1762issue
7issn
2161-5063journal_volume
9pub_type
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