Difference between revisions of "3-phosphoglycerate kinase"

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== Rate equation ==
 
== Rate equation ==
  
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Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used.  Since
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Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are 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{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} } </math></center>
  
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== Parameter values ==
  
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<center><math> \frac{V_{mf}\frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} } </math></center>
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{|class="wikitable"
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! Parameter
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! Value
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! Organism
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! Remarks
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|-
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|<math>V_{mf}</math>
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|13 <ref name="Hernandez_2006"> 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([http://dx.doi.org/doi:10.1111/j.1742-4658.2006.05214.x doi]) </ref>
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|rowspan="6"|HeLa cell line
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|rowspan="6"|
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|-
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|<math>V_{mr}</math>
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|3.8<ref name="Hernandez2011"></ref>
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|-
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|<math>Km_{1,3BPG}</math>
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|0.079<ref name="Hernandez2011"></ref>
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|-
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|<math>Km_{3PG}</math>
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|0.13<ref name="Hernandez2011"></ref>
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|-
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|<math>Km_{ADP}</math>
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|0.04<ref name="Hernandez2011"></ref>
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|-
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|<math>Km_{ATP}</math>
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|0.27<ref name="Hernandez2011"></ref>
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|}
  
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== Parameter values ==
 
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Checking references<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>
 
 
== Alternative parameter values ==
 
== Alternative parameter values ==
  

Revision as of 16:01, 4 March 2014

Phosphoglycerate kinase (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Like all kinases it is a transferase.

Chemical equation

1,3BPG + ADP \rightleftharpoons 3PG + ATP


Rate equation

Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used. [1]

\frac{V_{mf}\frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} }

Parameter values

Parameter Value Organism Remarks
V_{mf} 13 [2] HeLa cell line
V_{mr} 3.8[1]
Km_{1,3BPG} 0.079[1]
Km_{3PG} 0.13[1]
Km_{ADP} 0.04[1]
Km_{ATP} 0.27[1]

Alternative parameter values

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Marín-Hernández A, Gallardo-Pérez JC, Rodríguez-Enríquez S et al (2011) Modeling cancer glycolysis. Biochim Biophys Acta 1807:755–767 (doi)
  2. ↑ 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)
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