Difference between revisions of "Enolase"

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(Created page with "'''Enolase''', also known as phosphopyruvate hydratase, catalysis the conversion of [http://en.wikipedia.org/wiki/2-phosphoglycerate 2-phosphoglycerate] (2-PG) to [http://en.w...")
 
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'''Enolase''', also known as phosphopyruvate hydratase, catalysis the conversion of [http://en.wikipedia.org/wiki/2-phosphoglycerate 2-phosphoglycerate] (2-PG) to [http://en.wikipedia.org/wiki/Phosphoenolpyruvate phosphoenolpyruvate] (PEP). This is the penultimate step of glycolysis.
 
'''Enolase''', also known as phosphopyruvate hydratase, catalysis the conversion of [http://en.wikipedia.org/wiki/2-phosphoglycerate 2-phosphoglycerate] (2-PG) to [http://en.wikipedia.org/wiki/Phosphoenolpyruvate phosphoenolpyruvate] (PEP). This is the penultimate step of glycolysis.
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==Chemical equation==
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<center><math>2PG \rightleftharpoons PEP</math></center>
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==Rate equation==
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Mono-substrate reversible Michaelis-Menten equation is used. <ref name="Hernandez2011"> Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 ([http://dx.doi.org/10.1016/j.bbabio.2010.11.006 doi])  </ref>
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<center><math> \frac{V_{mf}\frac{[2PG]}{K_{2PG}}-V_{mr}\frac{[PEP]}{K_{PEP}}}{1 + \frac{[2PG]}{K_{2PG}} + \frac{[PEP]}{K_{PEP}}}  </math></center>
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==Parameter values==
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==Alternative parameter values==
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==References==
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<references/>

Revision as of 15:59, 27 February 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.

Chemical equation

2PG \rightleftharpoons PEP

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}}}

Parameter values

Alternative parameter values

References

  1. Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)