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Main Title: Dynamic Modelling of Phosphorolytic Cleavage Catalyzed by Pyrimidine-Nucleoside Phosphorylase
Author(s): Giessmann, Robert T.
Krausch, Niels
Kaspar, Felix
Cruz-Bournazou, Mariano Nicolas
Wagner, Anke
Neubauer, Peter
Gimpel, Matthias
Type: Article
Language Code: en
Abstract: Pyrimidine-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.
Issue Date: 19-Jun-2019
Date Available: 25-Jun-2019
DDC Class: 570 Biowissenschaften; Biologie
Subject(s): enzymatic reaction
reversible reaction
dynamic modelling
pyrimidine-nucleoside phosphorylase
spectroscopic assay
process kinetics
ODE model
Sponsor/Funder: DFG, 414044773, Open Access Publizieren 2019 - 2020 / Technische Universität Berlin
DFG, 390540038, EXC 2008: Vereinigung von Systemen in der Katalyse
Journal Title: Processes
Publisher: MDPI
Publisher Place: Basel
Volume: 7
Issue: 6
Article Number: 380
Publisher DOI: 10.3390/pr7060380
EISSN: 2227-9717
Appears in Collections:FG Bioverfahrenstechnik » Publications

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