Enzymology of the C8-Oxylipin Biosynthesis in Cyclocybe aegerita
dc.contributor.advisor | Rühl, Martin | |
dc.contributor.advisor | Sträßer, Katja | |
dc.contributor.advisor | Wegner, Hermann | |
dc.contributor.advisor | Schäberle, Till | |
dc.contributor.author | Karrer, Dominik | |
dc.date.accessioned | 2022-09-19T14:32:13Z | |
dc.date.available | 2022-09-19T14:32:13Z | |
dc.date.issued | 2022 | |
dc.description.abstract | Based on transcriptomic, volatilomic and metabolomic data of the model organism Cyclocybe aegerita, the endogenous and enzymatic production of the C8-oxylipins oct-2-en-1-ol, octan-1-ol, oct-2-enal, octanal, octan-3-ol, oct-1-en-3-ol, oct-1-en-3-one and octan-3-one via biotransformations with [U-13C]linoleic acid was compared to the developmental state depending gene expression patterns of putative oxylipin-associated enzyme classes like lipoxygenases, dioxygenases, ene-reductases and alcohol dehydrogenases. On closer consideration of these data sets, the C8-oxylipin production seemed to occur cluster-like. While one cluster (ketonic-cycle) consisted of octan-3-ol, oct-1-en-3-one, octan-3-one and oct-1-en-3-ol, which were detected through out all developmental stages, a second cluster (aldehydic-cycle) primarily active at early developmental stages involved oct-2-enal, octanal, oct-2-en-1-ol and octan-1-ol. Studying these clusters revealed that all C8-oxylipins of the aldehydic-cycle and ketonic-cycle can be derived from oct-2-enal and oct-1-en-3-one, respectively. A detailled consideration of the gene expression patterns revealed several enzyme classes putatively involved in the C8-oxylipin biosynthesis. Especially the two genes AAE3 04864 and AAE3 13549 encoding the lox4- and enr1-gene showed great similarities between their strongly increasing transcript counts with maturation. Subsequent recombinant production of CaeLOX4 and CaeEnR1 revealed that CaeLOX4 showed a preference for C18-fatty acids with the highest affinity towards linoleic acid. Analysis of the reaction product revealed that this LOX selectively oxygenated linoleic acid at position 13 to 13-hydroperoxyoctadecadienoic acid (13-HPOD). CaeEnR1 showed high affinities towards the reduction of oct-1-en-3-one and oct-2-enal to their saturated counterparts octan-3-one and octanal, respectively. Due to the strong similarities between the expression patterns of CaeLOX4 and CaeEnR1 a coherence between their main reaction products 13-HPOD and the precursor of the ketonic-cycle oct-1-en-3-one seems very likely. This suggests a biosynthetic route from linoleic acid to 13-HPOD, followed by a subsequent cleavage step to oct-1-en-3-one and therefore to C8-oxylipins of the ketonic-cycle. | de_DE |
dc.identifier.uri | https://jlupub.ub.uni-giessen.de//handle/jlupub/7719 | |
dc.identifier.uri | http://dx.doi.org/10.22029/jlupub-7151 | |
dc.language.iso | en | de_DE |
dc.relation.haspart | https://doi.org/10.1371/journal.pone.0218625 | de_DE |
dc.relation.haspart | https://doi.org/10.1007/s11557-021-01719-3 | de_DE |
dc.relation.haspart | https://doi.org/10.1002/cctc.202002011 | de_DE |
dc.relation.haspart | https://doi.org/10.1186/s13568-021-01195-8 | de_DE |
dc.rights | In Copyright | * |
dc.rights.uri | http://rightsstatements.org/page/InC/1.0/ | * |
dc.subject | enzymes | de_DE |
dc.subject | biosynthesis | de_DE |
dc.subject | oxylipins | de_DE |
dc.subject | 1-octen-3-ol | de_DE |
dc.subject | fungi | de_DE |
dc.subject.ddc | ddc:500 | de_DE |
dc.subject.ddc | ddc:540 | de_DE |
dc.subject.ddc | ddc:570 | de_DE |
dc.title | Enzymology of the C8-Oxylipin Biosynthesis in Cyclocybe aegerita | de_DE |
dc.type | doctoralThesis | de_DE |
dcterms.dateAccepted | 2022-09-13 | |
local.affiliation | FB 08 - Biologie und Chemie | de_DE |
thesis.level | thesis.doctoral | de_DE |
Dateien
Originalbündel
1 - 1 von 1
Lade...
- Name:
- KarrerDominik-2022-09-13.pdf
- Größe:
- 24.67 MB
- Format:
- Adobe Portable Document Format
- Beschreibung:
Lizenzbündel
1 - 1 von 1
Vorschaubild nicht verfügbar
- Name:
- license.txt
- Größe:
- 7.58 KB
- Format:
- Item-specific license agreed upon to submission
- Beschreibung: