Difference between revisions of "ATPase"

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==Parameters with uncertainty==
 
==Parameters with uncertainty==
* Three value of K for ATPase has been reported in Hernandez (2011) et. al. <ref name="Hernandez2011"></ref>: 0.0042, 0.0045 for Normoxia and 0.003 for Hypoxia. Taking the average and calculating the Std. Dev. the value is <math>0.0039 \pm 0.00079</math>
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* Three value of K for ATPase has been reported in Hernandez (2011) et. al. <ref name="Hernandez2011"></ref>: 0.0042, 0.0045 for Normoxia and 0.003 for Hypoxia. Taking the average and calculating the Std. Dev. the value is <math>0.0039 \pm 0.00079</math>. Hernandez (2011) et. al. <ref name="Hernandez2011"></ref> reported these values to be adjusted. As the Vmax values were reported in math>U\cdot(\text{mg protein})^{-1}</math>, therefore we adjust these value by multiplying with 65. This gives the value <math>0.2535 \pm 0.05</math>
  
 
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Latest revision as of 15:22, 28 October 2014


ATPases catalyze the decomposition of ATP into ADP and a free phosphate ion. [1]

Chemical reaction

 ATP \rightarrow ADP + Pi

Rate equation

Mass action rate law is used in which K was the rate constant and ATP was the substrate concentration

v = K \times [ATP]

Parameter values

Parameter Value Organism Remarks
K 3 \times 10^{-3} [2] HeLa cell line

Parameters with uncertainty

  • Three value of K for ATPase has been reported in Hernandez (2011) et. al. [2]: 0.0042, 0.0045 for Normoxia and 0.003 for Hypoxia. Taking the average and calculating the Std. Dev. the value is 0.0039 \pm 0.00079. Hernandez (2011) et. al. [2] reported these values to be adjusted. As the Vmax values were reported in math>U\cdot(\text{mg protein})^{-1}</math>, therefore we adjust these value by multiplying with 65. This gives the value 0.2535 \pm 0.05
Parameter Value Organism Remarks
K 0.2535 \pm 0.05 HeLa cell line

References

  1. Geider, K. and Hofmann-Berling, H. (1981). Proteins controlling the helical structure of DNA. Annu. Rev. Biochem. 50: 233–260.
  2. 2.0 2.1 2.2 Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)