ArticleFrontiers in bioengineering and biotechnology2022
Identification of key amino acid residues toward improving the catalytic activity and substrate specificity of plant-derived cytochrome P450 monooxygenases CYP716A subfamily enzyme for triterpenoid production in
Article in Frontiers in bioengineering and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Systematic enzyme and cofactor engineering for efficient ursolic acid biosynthesis inSynthetic and systems biotechnology · 2027Article
- Advances in the heterologous biosynthesis of QS saponins: a review.Microbial cell factories · 2026Review
- Roles of three cytochrome P450 monooxygenases in triterpene biosynthesis and their potential impact on growth and development.Plant physiology · 2024Article
- Heterologous production of corosolic acid, a phyto-insulin, in agroinfiltratedPlant biotechnology (Tokyo, Japan) · 2024Article
- Transcriptome analysis revealing the effect ofHeliyon · 2024Article
- Article
- High-yield bioactive triterpenoid production by heterologous expression inFrontiers in plant science · 2022Article
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Authors and funding
5 authors.
Funding
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Abstract
Triterpenoids constitute a group of specialized plant metabolites with wide structural diversity and high therapeutic value for human health. Cytochrome P450 monooxygenases (CYP) are a family of enzymes important for generating the structural diversity of triterpenoids by catalyzing the site-specific oxidization of the triterpene backbone. The CYP716 enzyme family has been isolated from various plant families as triterpenoid oxidases; however, their experimental crystal structures are not yet available and the detailed catalytic mechanism remains elusive. Here, we address this challenge by integrating bioinformatics approaches with data from other CYP families.
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