ArticlePhytochemistry2021
A pair of threonines mark ent-kaurene synthases for phytohormone biosynthesis.
Article in Phytochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Genome-wide analysis of terpene synthase family in peanut (Arachis hypogaea L.) explores the potential cross-talk in terpenoid biosynthesis.BMC genomics · 2025Article
- Identification of Cumin (Plants (Basel, Switzerland) · 2023Article
- Structural Understanding of Fungal Terpene Synthases for the Formation of Linear or Cyclic Terpene Products.ACS catalysis · 2023Article
- Plant (di)terpenoid evolution: from pigments to hormones and beyond.Natural product reports · 2023Review
- Origin and early evolution of the plant terpene synthase family.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
All land plants (embryophytes) must contain an ent-kaurene synthase (KS), as the ability to produce this olefin from ent-copalyl diphosphate (ent-CPP) is required for phytohormone biosynthesis. These KSs have frequently given rise to other class I diterpene synthases that catalyze distinct reactions for more specialized plant metabolism. Indeed, the prevalence of such gene duplication and neofunctionalization has obscured phylogenetic assignment of function. Here a pair of threonines is found to be conserved in all land plant KS involved in phytohormone biosynthesis, and their role in enzyme function investigated. Surprisingly, these threonines are not required, nor even particularly important for efficient production of ent-kaurene from ent-CPP. In addition, these threonines do not seem to affect protein structure or stability. Moreover, the absence of codon bias and positioning within an intron do not support a role in transcription or translation either. Despite their lack of apparent function, this pair of threonines are nevertheless completely conserved in all embryophyte KS from phytohormone biosynthesis. Thus, regardless of exact role, this serves as a diagnostic mark for such KS, enabling more confident distinction of these critical enzymes.
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