Difference between revisions of "UDPG-pyrophosphorylase"
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|Dimensionless | |Dimensionless | ||
|} | |} | ||
+ | |||
+ | |||
+ | ==Parameters with uncertainty== | ||
+ | * The value of <math>V_{max}</math> is reported to be <math>9.6 %</math> of <math>V_{max, PGLM}</math>. The Std. Dev. for <math>V_{max, PGLM}</math> was considered to be <math>10.5%</math> of its mean value. Same error percentage is considered for <math>V_{max}</math>. | ||
+ | |||
+ | {|class="wikitable" | ||
+ | ! Parameter | ||
+ | ! Value | ||
+ | ! Units | ||
+ | ! Organism | ||
+ | ! Remarks | ||
+ | |- | ||
+ | |<math>V_{max}</math> | ||
+ | |<math>200 \pm 21</math> <ref name = "villar_1960"> Villar-Palasi C & Larner J (1960). ''Levels of activity of the enzymes of the glycogen cycle in rat tissues''. Arch Biochem Biophys 86, 270–273.</ref> | ||
+ | |<math>min^{-1}</math> | ||
+ | |rowspan="6"|Recombinant, human muscle | ||
+ | |rowspan="6"| | ||
+ | |- | ||
+ | |<math>K_{Glc1P}</math> | ||
+ | |<math> 0.4 \pm 0.051 </math> <ref name="duggleby_1996"> Duggleby RG, Chao YC, Huang JG, Peng HL & Chang HY (1996). ''Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli''. Eur J Biochem 235, 173–179. </ref> | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>K_{UTP}</math> | ||
+ | |<math>0.97 \pm 0.08</pm> <ref name="duggleby_1996"></ref> | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>K_{UDPG}</math> | ||
+ | |<math> 0.063 \pm 0.006 </math> <ref name="duggleby_1996"></ref> | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>K_{ppi}</math> | ||
+ | |<math>0.38 \pm 0.036</math><ref name="duggleby_1996"></ref> | ||
+ | |mM | ||
+ | |- | ||
+ | |<math>K_{eq}</math> | ||
+ | |<math>0.24</math><ref name="duggleby_1996"></ref> | ||
+ | |Dimensionless | ||
+ | |} | ||
+ | |||
==References== | ==References== | ||
<references/> | <references/> |
Revision as of 11:57, 8 May 2014
This enzyme converts UTP and G1P to UDP-glucose (UDPG) and pyrophosphate (PPi)
Contents
Chemical equation
Rate equation
Reversible Bi substrate Michaelis-Menten equation with random binding order is used [1]
Parameter values
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
200 [2] | Recombinant, human muscle | |||
0.4 [3] | mM | |||
0.92 [3] | mM | |||
[3] | mM | |||
[3] | mM | |||
[3] | Dimensionless |
Parameters with uncertainty
- The value of is reported to be of . The Std. Dev. for was considered to be of its mean value. Same error percentage is considered for .
Parameter | Value | Units | Organism | Remarks |
---|---|---|---|---|
[2] | Recombinant, human muscle | |||
[3] | mM | |||
Failed to parse (lexing error): 0.97 \pm 0.08</pm> <ref name="duggleby_1996"></ref> |mM |- |<math>K_{UDPG} | [3] | mM | ||
[3] | mM | |||
[3] | Dimensionless |
References
- ↑ Palm, D.C. (2013). The regulatory design of glycogen metabolism in mammalian skeletal muscle (Ph.D.). University of Stellenbosch
- ↑ 2.0 2.1 Villar-Palasi C & Larner J (1960). Levels of activity of the enzymes of the glycogen cycle in rat tissues. Arch Biochem Biophys 86, 270–273.
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 3.6 3.7 3.8 Duggleby RG, Chao YC, Huang JG, Peng HL & Chang HY (1996). Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli. Eur J Biochem 235, 173–179.