Difference between revisions of "3-phosphoglycerate kinase"
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== Parameter values == | == Parameter values == | ||
− | Checking references<ref name=" | + | 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 15:18, 27 February 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.
Contents
Chemical equation
![1,3BPG + ADP \rightleftharpoons 3PG + ATP](/wiki/images/math/c/3/9/c39a15c314413cab0ee1c050fc4b274f.png)
Rate equation
Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used. Since
![\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}} }](/wiki/images/math/8/e/b/8eb366ea68004741a7ace7e2cf32d509.png)
Parameter values
Checking references[1]