Reaction mechanism of the farnesyl pyrophosphate C-methyltransferase towards the biosynthesis of pre-sodorifen pyrophosphate by Serratia plymuthica 4Rx13.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
04 02 2021
Historique:
received: 30 10 2020
accepted: 18 01 2021
entrez: 5 2 2021
pubmed: 6 2 2021
medline: 20 11 2021
Statut: epublish

Résumé

Classical terpenoid biosynthesis involves the cyclization of the linear prenyl pyrophosphate precursors geranyl-, farnesyl-, or geranylgeranyl pyrophosphate (GPP, FPP, GGPP) and their isomers, to produce a huge number of natural compounds. Recently, it was shown for the first time that the biosynthesis of the unique homo-sesquiterpene sodorifen by Serratia plymuthica 4Rx13 involves a methylated and cyclized intermediate as the substrate of the sodorifen synthase. To further support the proposed biosynthetic pathway, we now identified the cyclic prenyl pyrophosphate intermediate pre-sodorifen pyrophosphate (PSPP). Its absolute configuration (6R,7S,9S) was determined by comparison of calculated and experimental CD-spectra of its hydrolysis product and matches with those predicted by semi-empirical quantum calculations of the reaction mechanism. In silico modeling of the reaction mechanism of the FPP C-methyltransferase (FPPMT) revealed a S

Identifiants

pubmed: 33542330
doi: 10.1038/s41598-021-82521-9
pii: 10.1038/s41598-021-82521-9
pmc: PMC7862628
doi:

Substances chimiques

1,2,4,5,6,7,8-heptamethyl-3-methylenebicyclo(3.2.1)oct-6-ene 0
Bacterial Proteins 0
Bridged Bicyclo Compounds 0
Octanes 0
Polyisoprenyl Phosphates 0
Recombinant Proteins 0
Sesquiterpenes 0
geranyl pyrophosphate 763-10-0
farnesyl pyrophosphate 79W6B01D07
Methyltransferases EC 2.1.1.-
geranylgeranyl pyrophosphate N21T0D88LX

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

3182

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Auteurs

Marie Chantal Lemfack (MC)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany. marie.lemfack@uni-rostock.de.

Wolfgang Brandt (W)

Department of Bioorganic Chemistry, Leibniz-Institute of Plant Biochemistry, Weinberg 3, 06120, Halle, Germany. Wolfgang.Brandt@ipb-halle.de.

Katja Krüger (K)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany.
Department of Internal Medicine I, University Hospital RWTH Aachen, 52074, Aachen, Germany.

Alexandra Gurowietz (A)

Department of Bioorganic Chemistry, Leibniz-Institute of Plant Biochemistry, Weinberg 3, 06120, Halle, Germany.
Institute of Biology, Martin-Luther-Universität Halle-Wittenberg, Weinberg 10, 06120, Halle (Saale), Germany.

Jacky Djifack (J)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany.
PIMAN Consultants, 12 Rue Barthelemy Danjou, 92100, Boulogne-Billancourt, France.

Jan-Philip Jung (JP)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany.

Marius Hopf (M)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany.
Duale Hochschule Gera-Eisenach, Weg der Freundschaft 4, 07546, Gera, Germany.

Heiko Noack (H)

Institute of Pharmacy/Biosynthesis of Active Substances, Hoher Weg 8, 06120, Halle (Saale), Germany.

Björn Junker (B)

Institute of Pharmacy/Biosynthesis of Active Substances, Hoher Weg 8, 06120, Halle (Saale), Germany.

Stephan von Reuß (S)

Laboratory of Bioanalytical Chemistry, Institute of Chemistry, University of Neuchatel, Avenue de Bellevaux 51, 2000, Neuchâtel, Switzerland.

Birgit Piechulla (B)

Institute of Biological Sciences, University of Rostock, Albert-Einstein-Straße 3, 18059, Rostock, Germany.

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