Difference between revisions of "Phosphoglycerate dehydrogenase"

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==Parameters with uncertainty==
 
==Parameters with uncertainty==
*serA is the enzyme concentration collected from Turnaev 'et. al.' <ref name="Turnaev_2006"></ref> which is considered to be fixed.
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*serA is the enzyme concentration collected from Turnaev ''et. al.'' <ref name="Turnaev_2006"></ref> which is considered to be fixed.
  
 
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==References==
 
==References==
 
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<references/>

Revision as of 13:07, 6 May 2014


The enzyme Phosphoglycerate dehydrogenase (PDH) catalyzes the reaction to convert 3-phospho-D-glycerate (P3G) to phosphonooxypyruvate (PHP). The cofactors NADH and NAD+.

Chemical equation

3PG \rightleftharpoons PHP

Rate equation

Modified rate equation is used [1]

Failed to parse (Cannot store math image on filesystem.): \frac{ serA*KcatA*\frac{[3PG]}{KA_{3PG}}}{\frac{1 + \frac{[3PG]}{KA_{3PG}} + \frac{[PHP]}{KA_{PHP}} }{1+ \frac{[SER]}{KiA_{SER}}}}

Parameters

Parameter Value Units Organism Remarks
serA 1.15 [2] mM Escherichia coli
KcatA 0.55 [3] 1/s
Ka_{3PG} 1.2[3] mM
Ka_{PHP} 0.0032[3] mM
KiA_{SER} 0.0038[3] mM

Parameters with uncertainty

  • serA is the enzyme concentration collected from Turnaev et. al. [2] which is considered to be fixed.
Parameter Value Units Organism Remarks
serA 1.15 [2] mM Escherichia coli
KcatA 0.55 [3] 1/s
Ka_{3PG} 1.2[3] mM
Ka_{PHP} 0.0032[3] mM
KiA_{SER} 0.0038[3] mM

References

  1. Smallbone K, Stanford NJ (2013). Kinetic modeling of metabolic pathways: Application to serine biosynthesis. In: Systems Metabolic Engineering, Humana Press. pp. 113–121
  2. 2.0 2.1 2.2 Turnaev II, Ibragimova SS, Usuda Y et al (2006). Mathematical modeling of serine and glycine synthesis regulation in Escherichia coli. Proceedings of the fifth international conference on bioinformatics of genome regulation and structure 2:78–83
  3. 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 Zhao G, Winkler ME (1996). A novel alphaketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria. J Bacteriol 178:232–239