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  Characterization of maximal enzyme catalytic rates in central metabolism of Arabidopsis thaliana

Küken, A., Gennermann, K., & Nikoloski, Z. (2020). Characterization of maximal enzyme catalytic rates in central metabolism of Arabidopsis thaliana. The Plant Journal, 103(6), 2168-2177. doi:10.1111/tpj.14890.

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Küken, A.1, Author              
Gennermann, Kristin2, Author
Nikoloski, Z.1, Author              
Affiliations:
1Mathematical Modelling and Systems Biology - Nikoloski, Cooperative Research Groups, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753310              
2External Organizations, ou_persistent22              

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Free keywords: enzyme catalytic rates, constraint-based modeling, Arabidopsis thaliana, kinetic parameter, metabolic network, turnover number
 Abstract: Summary Availability of plant-specific enzyme kinetic data is scarce, limiting the predictive power of metabolic models and precluding identification of genetic factors of enzyme properties. Enzyme kinetic data are measured in vitro, often under nonphysiological conditions, and conclusions elicited from modeling warrant caution. Here we estimate maximal in vivo catalytic rates for 168 plant enzymes, including photosystems I and II, cytochrome-b6f complex, ATP-citrate synthase, sucrose-phosphate synthase as well as enzymes from amino acid synthesis with previously undocumented enzyme kinetic data in BRENDA. The estimations are obtained by integrating condition-specific quantitative proteomics data, maximal rates of selected enzymes, growth measurements from Arabidopsis thaliana rosette with and fluxes through canonical pathways in a constraint-based model of leaf metabolism. In comparison to findings in Escherichia coli, we demonstrate weaker concordance between the plant-specific in vitro and in vivo enzyme catalytic rates due to a low degree of enzyme saturation. This is supported by the finding that concentrations of nicotinamide adenine dinucleotide (phosphate), adenosine triphosphate, and uridine triphosphate, calculated based on our maximal in vivo catalytic rates, and available quantitative metabolomics data are below reported KM values and therefore, indicate undersaturation of respective enzymes. Our findings show that genome-wide profiling of enzyme kinetic properties is feasible in plants, paving the way for understanding resource allocation.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1111/tpj.14890
BibTex Citekey: doi:10.1111/tpj.14890
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Title: The Plant Journal
  Other : Plant J.
Source Genre: Journal
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Publ. Info: Oxford : Blackwell Science
Pages: - Volume / Issue: 103 (6) Sequence Number: - Start / End Page: 2168 - 2177 Identifier: ISSN: 0960-7412
CoNE: https://pure.mpg.de/cone/journals/resource/954925579095_1