3-phosphoglycerate kinase
3-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. [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}} }](/wiki/images/math/8/e/b/8eb366ea68004741a7ace7e2cf32d509.png)
Parameter values
Parameter | Value | Units | Organism | Remarks |
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8.7 [2] | ![]() |
HeLa cell line | |
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2.5[1] | ![]() | ||
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0.079[1] | mM | ||
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0.13[1] | mM | ||
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0.04[1] | mM | ||
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0.27[1] | mM |
Parameters with uncertainty
Parameter | Value | Units | Organism | Remarks |
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Human | |
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Failed to parse (Cannot store math image on filesystem.): 833 \pm 50 | ![]() | ||
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mM | ||
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mM | ||
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mM | ||
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mM |
References
- ↑ 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)
- ↑ 2.0 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 3.3 Szabo, J.; Varga, A.; Flachner, B.; Konarev, P.V.; Svergun, D.I.; Zavodszky, P.; Vas, M. (2008), Role of side-chains in the operation of the main molecular hinge of 3-phosphoglycerate kinase, FEBS Lett. 582, 1335-1340