Lactococcus lactis glycolysis

Detailed kinetic model for glycolysis of L. lactis. The model is basically the same model as that published by Hoefnagel et al 2002 (Mol. Biol. Reports 29, 157-161). The change made to the model is to make external glucose a variable such that a glucose pulse can be simulated.

Creators: Jacky Snoep, Ana Rute Neves

Submitter: Katy Wolstencroft

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COGEME_extraction_mod-chemostat_v1

Biomass samples (20ml) were taken via the sample port of the Applikon fermenters. The cells were pelleted by centrifugation for 5min at 5000rpm. The supernatant was removed and the RNA pellet resuspended in the residual medium to form a slurry. This was added in a dropwise manner directly into a 5ml Teflon flask (B. Braun Biotech, Germany) containing liquid nitrogen and a 7mm-diameter tungsten carbide ball.

Taken from ArrayExpress: http://www.ebi.ac.uk/microarray-as/ae/browse.html?keywords=E-MEXP-115 ...

Creator: Katy Wolstencroft

Submitter: Katy Wolstencroft

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Can yeast glycolysis be understood in terms of in vitro kinetics of the constituent enzymes? Testing biochemistry

Abstract (Expand)

This paper examines whether the in vivo behavior of yeast glycolysis can be understood in terms of the in vitro kinetic properties of the constituent enzymes. In nongrowing, anaerobic, compressed … Saccharomyces cerevisiae the values of the kinetic parameters of most glycolytic enzymes were determined. For the other enzymes appropriate literature values were collected. By inserting these values into a kinetic model for glycolysis, fluxes and metabolites were calculated. Under the same conditions fluxes and metabolite levels were measured. In our first model, branch reactions were ignored. This model failed to reach the stable steady state that was observed in the experimental flux measurements. Introduction of branches towards trehalose, glycogen, glycerol and succinate did allow such a steady state. The predictions of this branched model were compared with the empirical behavior. Half of the enzymes matched their predicted flux in vivo within a factor of 2. For the other enzymes it was calculated what deviation between in vivo and in vitro kinetic characteristics could explain the discrepancy between in vitro rate and in vivo flux.

Authors: Firstname Lastname, J Passarge, C A Reijenga, E Esgalhado, C C van der Weijden, M Schepper, M C Walsh, B M Bakker, K van Dam, H V Westerhoff, Firstname Lastname

Date Published: 22nd Aug 2000

Publication Type: Not specified

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Creators: Quyen Yamanaka, dddd

Submitter: Quyen Yamanaka

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