Difference between revisions of "Enolase"
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− | * Three values for <math>Km_{ | + | * Three values for <math>Km_{2PG}</math> is collected. The values are 0.20 <ref name="Pietkiewicz_2009">Pietkiewicz, J., Gamian, A., Staniszewska, M., & Danielewicz, R. (2009), ''Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products'', Journal of Enzyme Inhibition and Medicinal Chemistry, 24, 356–364</ref>, 0.199 <ref name="Pietkiewicz_2009"></ref>, 0.038 <ref name="Hernandez2011"></ref>. The mean and std. dev. is <math>0.145 \pm 0.07</math> |
+ | |||
+ | * Similarly for <math>Km_{PEP}</math> three reported values are 0.58, 0.702, 0.06. The uncertainty is then <math>0.44 \pm 0.276</math>. | ||
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+ | * In Pietkiewicz et. al. (2009) <ref name="Pietkiewicz_2009"></ref> <math>V_{mr}</math> is reported as 1.4 <math>mmol/min^{-1}</math> and Marín-Hernández et. al. (2011) reported it to be 0.4. The mean and the std. dev. calculated from these two values are <math>0.9 \pm 0.5</math>. | ||
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{|class="wikitable" | {|class="wikitable" | ||
! Parameter | ! Parameter |
Revision as of 16:38, 29 April 2014
Enolase, also known as phosphopyruvate hydratase, catalysis the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP). This is the penultimate step of glycolysis.
Contents
Chemical equation
![2PG \rightleftharpoons PEP](/wiki/images/math/e/3/6/e36e43bdcf85d82cfe2a632b8567be12.png)
Rate equation
Mono-substrate reversible Michaelis-Menten equation is used. [1]
![\frac{V_{mf}\frac{[2PG]}{K_{2PG}}-V_{mr}\frac{[PEP]}{K_{PEP}}}{1 + \frac{[2PG]}{K_{2PG}} + \frac{[PEP]}{K_{PEP}}}](/wiki/images/math/6/a/9/6a9ca37a2fd76b4eb56a1e6a5cfb67d0.png)
Parameter values
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
![]() |
0.34 [2] | ![]() |
HeLa cell line | |
![]() |
0.38[1] | ![]() | ||
![]() |
0.038[1] | mM | ||
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0.06[1] | mM |
Parameters with uncertainty
- Three values for
is collected. The values are 0.20 [3], 0.199 [3], 0.038 [1]. The mean and std. dev. is
- Similarly for
three reported values are 0.58, 0.702, 0.06. The uncertainty is then
.
- In Pietkiewicz et. al. (2009) [3]
is reported as 1.4
and Marín-Hernández et. al. (2011) reported it to be 0.4. The mean and the std. dev. calculated from these two values are
.
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
![]() |
![]() |
![]() |
HeLa cell line | |
![]() |
![]() |
![]() | ||
![]() |
![]() |
mM | ||
![]() |
![]() |
mM |
References
- ↑ 1.0 1.1 1.2 1.3 1.4 Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)
- ↑ 2.0 2.1 Marín-Hernández A , Rodríguez-Enríquez S, Vital-González P A, et al. (2006). Determining and understanding the control of glycolysis in fast-growth tumor cells. Flux control by an over-expressed but strongly product-inhibited hexokinase. FEBS J., 273 , pp. 1975–1988(doi)
- ↑ 3.0 3.1 3.2 Pietkiewicz, J., Gamian, A., Staniszewska, M., & Danielewicz, R. (2009), Inhibition of human muscle-specific enolase by methylglyoxal and irreversible formation of advanced glycation end products, Journal of Enzyme Inhibition and Medicinal Chemistry, 24, 356–364