Dynamic Modelling of Phosphorolytic Cleavage Catalyzed by Pyrimidine-Nucleoside Phosphorylase

dc.contributor.authorGiessmann, Robert T.
dc.contributor.authorKrausch, Niels
dc.contributor.authorKaspar, Felix
dc.contributor.authorCruz-Bournazou, Mariano Nicolas
dc.contributor.authorWagner, Anke
dc.contributor.authorNeubauer, Peter
dc.contributor.authorGimpel, Matthias
dc.date.accessioned2019-06-25T09:30:05Z
dc.date.available2019-06-25T09:30:05Z
dc.date.issued2019-06-19
dc.description.abstractPyrimidine-nucleoside phosphorylases (Py-NPases) have a significant potential to contribute to the economic and ecological production of modified nucleosides. These can be produced via pentose-1-phosphates, an interesting but mostly labile and expensive precursor. Thus far, no dynamic model exists for the production process of pentose-1-phosphates, which involves the equilibrium state of the Py-NPase catalyzed reversible reaction. Previously developed enzymological models are based on the understanding of the structural principles of the enzyme and focus on the description of initial rates only. The model generation is further complicated, as Py-NPases accept two substrates which they convert to two products. To create a well-balanced model from accurate experimental data, we utilized an improved high-throughput spectroscopic assay to monitor reactions over the whole time course until equilibrium was reached. We examined the conversion of deoxythymidine and phosphate to deoxyribose-1-phosphate and thymine by a thermophilic Py-NPase from Geobacillus thermoglucosidasius. The developed process model described the reactant concentrations in excellent agreement with the experimental data. Our model is built from ordinary differential equations and structured in such a way that integration with other models is possible in the future. These could be the kinetics of other enzymes for enzymatic cascade reactions or reactor descriptions to generate integrated process models.en
dc.description.sponsorshipDFG, 414044773, Open Access Publizieren 2019 - 2020 / Technische Universität Berlinen
dc.description.sponsorshipDFG, 390540038, EXC 2008: Vereinigung von Systemen in der Katalyseen
dc.identifier.eissn2227-9717
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/9543
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-8596
dc.language.isoenen
dc.relation.ispartof10.14279/depositonce-10629en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subject.ddc570 Biowissenschaften; Biologiede
dc.subject.otherenzymatic reactionen
dc.subject.otherreversible reactionen
dc.subject.otherdynamic modellingen
dc.subject.otherpyrimidine-nucleoside phosphorylaseen
dc.subject.otherspectroscopic assayen
dc.subject.otherprocess kineticsen
dc.subject.otherODE modelen
dc.titleDynamic Modelling of Phosphorolytic Cleavage Catalyzed by Pyrimidine-Nucleoside Phosphorylaseen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.articlenumber380en
dcterms.bibliographicCitation.doi10.3390/pr7060380en
dcterms.bibliographicCitation.issue6en
dcterms.bibliographicCitation.journaltitleProcessesen
dcterms.bibliographicCitation.originalpublishernameMDPIen
dcterms.bibliographicCitation.originalpublisherplaceBaselen
dcterms.bibliographicCitation.volume7en
tub.accessrights.dnbfreeen
tub.affiliationFak. 3 Prozesswissenschaften::Inst. Biotechnologie::FG Bioverfahrenstechnikde
tub.affiliation.facultyFak. 3 Prozesswissenschaftende
tub.affiliation.groupFG Bioverfahrenstechnikde
tub.affiliation.instituteInst. Biotechnologiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen

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