Characterization of maximal enzyme catalytic rates in central metabolism of Arabidopsis thaliana. (24th July 2020)
- Record Type:
- Journal Article
- Title:
- Characterization of maximal enzyme catalytic rates in central metabolism of Arabidopsis thaliana. (24th July 2020)
- Main Title:
- Characterization of maximal enzyme catalytic rates in central metabolism of Arabidopsis thaliana
- Authors:
- Küken, Anika
Gennermann, Kristin
Nikoloski, Zoran - 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 non‐physiological 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 K M values and, therefore, indicate undersaturation of respective enzymes. Our findings show that genome‐wide profiling of enzyme kineticSUMMARY: 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 non‐physiological 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 K M 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. Significance Statement: By using a constraint‐based modeling approach that integrates publically available proteomics data from Arabidopsis thaliana under 10 different conditions, we estimate maximal in vivo enzyme catalytic rates. Our study provides a comprehensive parameterization of a large‐scale model of Arabidopsis metabolism. … (more)
- Is Part Of:
- Plant journal. Volume 103:Number 6(2020)
- Journal:
- Plant journal
- Issue:
- Volume 103:Number 6(2020)
- Issue Display:
- Volume 103, Issue 6 (2020)
- Year:
- 2020
- Volume:
- 103
- Issue:
- 6
- Issue Sort Value:
- 2020-0103-0006-0000
- Page Start:
- 2168
- Page End:
- 2177
- Publication Date:
- 2020-07-24
- Subjects:
- Arabidopsis thaliana -- constraint‐based modeling -- enzyme catalytic rates -- kinetic parameter -- metabolic network -- turnover number
Plant molecular biology -- Periodicals
Plant cells and tissues -- Periodicals
Botany -- Periodicals
580 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-313X ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/tpj.14890 ↗
- Languages:
- English
- ISSNs:
- 0960-7412
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6519.200000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21707.xml