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BIOMD0000000282 - Chance1952_Catalase_Mechanism

 

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Reference Publication
Publication ID: 14953444
CHANCE B, GREENSTEIN DS, HIGGINS J, YANG CC.
The mechanism of catalase action. II. Electric analog computer studies.
Arch. Biochem. Biophys. 1952 Jun; 37(2): 322-339
  [more]
Model
Original Model: BIOMD0000000282.origin
Submitter: Kieran Smallbone
Submission ID: MODEL1010190001
Submission Date: 19 Oct 2010 11:30:41 UTC
Last Modification Date: 08 Apr 2016 16:53:00 UTC
Creation Date: 10 Oct 2010 10:10:10 UTC
Encoders:  Lukas Endler
   Kieran Smallbone
set #1
bqbiol:hasTaxon Taxonomy Equus caballus
set #2
bqbiol:isVersionOf Gene Ontology regulation of catalytic activity
set #3
bqbiol:hasVersion Gene Ontology catalase activity
set #4
bqbiol:occursIn Brenda Tissue Ontology erythrocyte
Notes

This model is described in the article:
The mechanism of catalase action. II. Electric analog computer studies.
Britton Chance, David S Greenstein, Joseph Higgins, CC Yang, Arch Biochem. 1952 37:322-39. PubmedID:14953444
Summary:
An electric analog computer has been constructed for a study of the kinetics of catalase action. This computer gives results for the formation and disappearance of the catalase-hydrogen peroxide complex that are in good agreement with the experimental data. The computer study verifies an approximate method for the computation of the velocity constant for the combination of hydrogen peroxide and catalase and justifies the simple formula used previously to compute the velocity constant for the reaction of the catalase-hydrogen peroxide complex with donor molecules. Finally, the computer data show that the binding of peroxide to catalase is a practically irreversible reaction.

The reaction of the enzyme-substrate complex, p, with the electron donor, a, is bimolecular, although in the article, as a is assumed to be constant, it is modelled using an apparent rate constant consisting of the product of the rate constant, k4, and the concentration of a. In this implementation, the concentration of a is set to 1 and the value of k4 just adapted so that the product equals the values given for k4*a in the article. The specific parameter values are taken from Fig 3. The graphs do not exactly match those in the paper, this may be due to the different simulators used.

Model
Publication ID: 14953444 Submission Date: 19 Oct 2010 11:30:41 UTC Last Modification Date: 08 Apr 2016 16:53:00 UTC Creation Date: 10 Oct 2010 10:10:10 UTC
Mathematical expressions
Reactions
r1 r2 r3  
Physical entities
Compartments Species
cell enzyme E (catalase) substrate S (hydrogen peroxide) enzyme-substrate complex ES (catalase - hydrogen peroxide)
product 1 donor AH2 product 2
Global parameters
k1 k2 k4_prime k4
 cell Spatial dimensions: 3.0  Compartment size: 1.0
 
 enzyme E (catalase)
Compartment: cell
Initial concentration: 1.36
 
 substrate S (hydrogen peroxide)
Compartment: cell
Initial concentration: 2.0
 
 enzyme-substrate complex ES (catalase - hydrogen peroxide)
Compartment: cell
Initial concentration: 0.0
 
 product 1
Compartment: cell
Initial concentration: 0.0
 
 donor AH2
Compartment: cell
Initial concentration: 0.0
Constant
 
 product 2
Compartment: cell
Initial concentration: 0.0
 
Global Parameters (4)
 
 k1
Value: 11.0   (Units: per micromolar per second)
Constant
 
 k2
Constant
 
 k4_prime
Value: 16.6   (Units: per micromolar per second)
Constant
 
 k4
Value: 0.72   (Units: per micromolar per second)
Constant
 
Representative curation result(s)
Representative curation result(s) of BIOMD0000000282

Curator's comment: (updated: 24 Nov 2010 22:34:13 GMT)

Reproduction of figure 3 of the original publication. The simulations were performed using SBML ODEsolver with varying initial concentrations of the substrate, hydrogen peroxide, x. The time courses are slightly different from the published ones, which most likely is due to the completely different integrators used.

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