Difference between revisions of "Glyceraldehyde-3-phosphate dehydrogenase"
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|<math>Km_{1,3BPG}</math> | |<math>Km_{1,3BPG}</math> | ||
− | |<math>0.013 \pm 0.0035</math | + | |<math>0.013 \pm 0.0035</math> |
|mM | |mM | ||
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|<math>Km_{NAD+}</math> | |<math>Km_{NAD+}</math> | ||
− | |<math>0.019 \pm 0.007</math | + | |<math>0.019 \pm 0.007</math> |
|mM | |mM | ||
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Revision as of 11:31, 29 April 2014
The Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) enzyme serves two functions in glycolytic pathway. First the enzyme transfers a hydrogen (H-) from glyceraldehyde phosphate (Gly3P) to the oxidizing agent Nicotinamide Adenine Dinucleotide (NAD+) to form NADH. Next it adds a phosphate (P) from the cytosol to the oxidized Gly3P to form 1, 3-bisphosphoglycerate.
Contents
Chemical equation
Rate equation
Ordererd Ter-Bi reversible Michaelis-Menten equation for non-interacting substrates. [1]
Parameters
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
0.58 [2] | HeLa cell line | |||
0.72[2] | ||||
0.19[1] | mM | |||
0.022[1] | mM | |||
0.09[1] | mM | |||
0.01[1] | mM | |||
29[1] | mM |
Parameters with uncertainty
- Four values of have been collected from Lambeir et. al. (1991)[3] for different organisms. for Trypanosoma brucei, for Homo sapiens, for Geobacillus stearothermophilus and for Oryctolagus cuniculus. Calculating mean and std. dev. from these 4 values gives
- Three values collected under different conditions from human cell is reported for in Ryzlak (1998) et. al. [4]. Those values are 0.01, 0.02, 0.027. The mean and Std. Dev. from these three values are
- Three values for have also been reported under different conditions from human cell in Ryzlak (1998) et. al. [4]. Those values are 0.01, 0.012, 0.018. The mean and Std. Dev. from these three values are
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
[2] | HeLa cell line | |||
(5)[2] | ||||
0.19[1] | mM | |||
mM | ||||
mM | ||||
mM | Multiple organism | |||
29[1] | mM |
References
- ↑ 1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7 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 2.2 2.3 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)
- ↑ Lambeir, A.M.; Loiseau, A.M.; Kuntz, D.A.; Vellieux, F.M.; Michels, P.A.M.; Opperdoes, F.R. (1991), The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes, Eur. J. Biochem. 198, 429-435
- ↑ 4.0 4.1 Ryzlak, M.T.; Pietruszko, R. (1998), Heterogeneity of glyceraldehyde-3-phosphate dehydrogenase from human brain, Biochim. Biophys. Acta 954, 309-324