DataEntryID 97
    General information
      Manuscript title: A model of yeast glycolysis based on a consistent kinetic characterisation of all its enzymes.
      PubMed ID: http://www.ncbi.nlm.nih.gov/pubmed/23831062
      Journal: FEBS Letters
      Year: 2013
      Authors: Kieran Smallbone, Hanan L. Messiha, Kathleen M. Carroll, Catherine L. Winder, Naglis Malys, Warwick B. Dunn, Ettore Murabito, Neil Swainston, Joseph O. Dada, Farid Khan, Pınar Pir, Evangelos Simeonidis, Irena Spasić, Jill Wishart, Dieter Weichart, Neil W. Hayes, Daniel Jameson, David S. Broomhead, Stephen G. Oliver, Simon J. Gaskell, John E.G. McCarthy, Norman W. Paton, Hans V. Westerhoff, Douglas B. Kell, Pedro Mendes
      Affiliations: Manchester Centre for Integrative Systems Biology, Manchester Institute of Biotechnology, The University of Manchester, UK
      Keywords: Glycolysis, Systems biology, Enzyme kinetic, Isoenzyme, Modelling
      Full text article: https://kimosys.org/rails/active_storage/blobs/eyJfcmFpbHMiOnsibWVzc2FnZSI6IkJBaHBBcm9FIiwiZXhwIjpudWxsLCJwdXIiOiJibG9iX2lkIn19--692e98cc8c4949fa3370c61abc71735cd37fabe5/Smallbone_2013.pdf
      Project name: not specified

    Experiment description
      Organism: Saccharomyces cerevisiae
      Strain: Y23925
      Data type: enzyme/protein concentrations
      Data units: molecules/cell
      Execution date: not specified

    Experimental details
      Temperature (°C): not specified
      pH: not specified
      Carbon source: glucose
      Culture mode: chemostat
      Process condition: aerobic
      Dilution rate (h⁻¹): µmax
      Working volume: not specified L
      Biomass concentration (g/L): monitored by measuring the electrical capacitance of the culture.
      Medium composition: not specified
      General protocol information: Measurement method: LC-MS/MS;
      Methods description: S. cerevisiae cells from 50 ml cultures were harvested by centrifugation for 5 min at 4000 g, and the cells mechanically disrupted using a mini bead‐beater (Biospec Products Inc., Bartlesville, USA; http://www.biospec.com/) yielding the cellular cytoplasmic soluble fraction for analysis. The latter was combined with known amounts of the recombinant labelled QconCAT protein (containing diagnostic peptides for the glycolytic enzymes [1]), and co‐digested to completion with trypsin. The resulting peptides were diluted and resolved over a linear incrementing solvent gradient by LC‐MS using a nanoACQUITY chromatograph (Waters MS Technologies) coupled to an LTQ‐Orbitrap XL (ThermoFisher Scientific). Automated data analysis and subsequent calculations were carried out using the QconCAT PrideWizard [2]. 
---------------------------------References----------------------------------
[1]  K.M. Carroll , D.M. Simpson , C.E. Eyers , C.G. Knight , P. Brownridge , W.B. Dunn , C.L. Winder , K. Lanthaler , P. Pir , N. Malys , D.B. Kell , S.G. Oliver , S.J. Gaskell , R.J. Beynon. Mol. Cell. Proteomics, 10, (2011), M111.007633. http://doi.org/dzvw3h
[2] WN. Swainston , D. Jameson , K. Carroll. Proteomics, 11, (2011), 329– 333. http://doi.org/bqc27q
      Data file: http://kimosys.org/repository/97/download?parameter=1209; 
      Alternative formats: no files uploaded

    Submission and curation
      Entered by: Administrator KiMoSys
      Created: 2018-07-15 21:24:27 UTC
      Updated: 2020-04-24 16:10:35 UTC
      Version: 4
      Status: (reviewed) 2018-07-15 21:24:40 UTC
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      Downloads: 99