Chemical diversity in angiosperms − monoterpene synthases control complex reactions that provide the precursors for ecologically and commercially important monoterpenoids

SUMMARY Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover...

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Published inThe Plant journal : for cell and molecular biology Vol. 119; no. 1; pp. 28 - 55
Main Authors Srividya, Narayanan, Kim, Hoshin, Simone, Raugei, Lange, Bernd Markus
Format Journal Article
LanguageEnglish
Published England Blackwell Publishing Ltd 01.07.2024
Society for Experimental Biology
Subjects
Angiospermae
Angiosperms
BASIC BIOLOGICAL SCIENCES
Biosynthesis
carbocation
chemistry
class
crystal structure
enzymatic control
Food industry
Food plants
hydrides
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Intermediates
Intramolecular Lyases
ligands
Magnoliopsida - enzymology
Magnoliopsida - genetics
Magnoliopsida - metabolism
mechanistic enzymology
Metabolites
molecular dynamics
monoterpene synthase
Monoterpenes - metabolism
Monoterpenoids
Pharmaceutical industry
Plant ecology
Plant Proteins - genetics
Plant Proteins - metabolism
quantum mechanics/molecular mechanics
Quenching
Substrates
carbocation
mechanistic enzymology
crystal structure
quantum mechanics/molecular mechanics
enzymatic control
molecular dynamics
monoterpene synthase
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Abstract SUMMARY Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries. Significance Statement Terpenoids form the largest class of plant specialized metabolites and monoterpene synthases are enzymes that catalyze critical reactions that contribute to this chemical diversity. This foundational review provides an overview of the complex catalytic mechanism of these enzymes and discusses their relevance in the context of the roles of terpenoids in plant ecology and the food, cosmetic, and pharmaceutical industries.
AbstractList Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries.
Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries.Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries.
SUMMARY Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries. Significance Statement Terpenoids form the largest class of plant specialized metabolites and monoterpene synthases are enzymes that catalyze critical reactions that contribute to this chemical diversity. This foundational review provides an overview of the complex catalytic mechanism of these enzymes and discusses their relevance in the context of the roles of terpenoids in plant ecology and the food, cosmetic, and pharmaceutical industries.
SUMMARYMonoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high chemical diversity in angiosperms. In addition to accomplishing a rate enhancement, these enzymes manage the formation and turnover of highly reactive carbocation intermediates formed from a prenyl diphosphate substrate. At each step along the reaction path, a cationic intermediate can be subject to cyclization, migration of a proton, hydride, or alkyl group, or quenching to terminate the sequence. However, enzymatic control of ligand folding, stabilization of specific intermediates, and defined quenching chemistry can maintain the specificity for forming a signature product. This review article will discuss our current understanding of how angiosperm MTSs control the reaction environment. Such knowledge allows inferences about the origin and regulation of chemical diversity, which is pertinent for appreciating the role of monoterpenoids in plant ecology but also for aiding commercial efforts that harness the accumulation of these specialized metabolites for the food, cosmetic, and pharmaceutical industries.
Author Srividya, Narayanan
Kim, Hoshin
Lange, Bernd Markus
Simone, Raugei
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  fullname: Srividya, Narayanan
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  organization: Washington State University
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  surname: Kim
  fullname: Kim, Hoshin
  organization: Physical and Computational Sciences Division, Pacific Northwest National Laboratory
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  surname: Simone
  fullname: Simone, Raugei
  organization: Physical and Computational Sciences Division, Pacific Northwest National Laboratory
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  orcidid: 0000-0001-6565-9584
  surname: Lange
  fullname: Lange, Bernd Markus
  email: lange-m@wsu.edu
  organization: Washington State University
BackLink https://www.ncbi.nlm.nih.gov/pubmed/38565299$$D View this record in MEDLINE/PubMed
https://www.osti.gov/biblio/2332906$$D View this record in Osti.gov
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CitedBy_id crossref_primary_10_1093_hr_uhae272
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Issue 1
Keywords carbocation
mechanistic enzymology
crystal structure
quantum mechanics/molecular mechanics
enzymatic control
molecular dynamics
monoterpene synthase
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USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division (CSGB)
SC0001553; AC05-75RL01830; DE‐SC0001553; DE‐AC05‐75RL01830; AC05-76RL01830
USDOE Office of Science (SC), Biological and Environmental Research (BER)
ORCID 0000-0001-6565-9584
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OpenAccessLink https://proxy.k.utb.cz/login?url=https://onlinelibrary.wiley.com/doi/abs/10.1111%2Ftpj.16743
PMID 38565299
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crossref_citationtrail_10_1111_tpj_16743
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PublicationDate July 2024
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  text: July 2024
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PublicationPlace England
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PublicationTitle The Plant journal : for cell and molecular biology
PublicationTitleAlternate Plant J
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Publisher Blackwell Publishing Ltd
Society for Experimental Biology
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Snippet SUMMARY Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with...
Monoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with particularly high...
SUMMARYMonoterpene synthases (MTSs) catalyze the first committed step in the biosynthesis of monoterpenoids, a class of specialized metabolites with...
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SubjectTerms Angiospermae
Angiosperms
BASIC BIOLOGICAL SCIENCES
Biosynthesis
carbocation
chemistry
class
crystal structure
enzymatic control
Food industry
Food plants
hydrides
INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Intermediates
Intramolecular Lyases
ligands
Magnoliopsida - enzymology
Magnoliopsida - genetics
Magnoliopsida - metabolism
mechanistic enzymology
Metabolites
molecular dynamics
monoterpene synthase
Monoterpenes - metabolism
Monoterpenoids
Pharmaceutical industry
Plant ecology
Plant Proteins - genetics
Plant Proteins - metabolism
quantum mechanics/molecular mechanics
Quenching
Substrates
Title Chemical diversity in angiosperms − monoterpene synthases control complex reactions that provide the precursors for ecologically and commercially important monoterpenoids
URI https://onlinelibrary.wiley.com/doi/abs/10.1111%2Ftpj.16743
https://www.ncbi.nlm.nih.gov/pubmed/38565299
https://www.proquest.com/docview/3073665483
https://www.proquest.com/docview/3031662826
https://www.proquest.com/docview/3153662421
https://www.osti.gov/biblio/2332906
Volume 119
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