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Team:UIUC Illinois/Project/Parts
From 2013.igem.org
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<b>Cardiobiotics Parts </b><br></p> | <b>Cardiobiotics Parts </b><br></p> | ||
| - | <p class="left"> <b> | + | <p class="left"> <b>Carnitine dehydrogenase (CDHcab) BBa_K1205000 </b><br> |
• Derived from <i>pseudomonas aeruginosa</i> strain PAO1 <br> | • Derived from <i>pseudomonas aeruginosa</i> strain PAO1 <br> | ||
• This gene codes for L-Carnitine Dehydrogenase, a protein that breaks down L-carnitine into 3-Dehydrocarnitine. This enzyme directs the degradation down a pathway that prevents the formation of trimethylamine. As previously mentioned trimethylamine has been known to cause cardiovascular disease. This new pathway ultimately leads to glycine which is a nature substance in the body. This enzyme is the centerpiece of our experiment. <br> | • This gene codes for L-Carnitine Dehydrogenase, a protein that breaks down L-carnitine into 3-Dehydrocarnitine. This enzyme directs the degradation down a pathway that prevents the formation of trimethylamine. As previously mentioned trimethylamine has been known to cause cardiovascular disease. This new pathway ultimately leads to glycine which is a nature substance in the body. This enzyme is the centerpiece of our experiment. <br> | ||
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| - | <b> | + | <b>cbcVW</b> |
• From <i>pseudomonas aeruginosa</i> strain PAO1 <br> | • From <i>pseudomonas aeruginosa</i> strain PAO1 <br> | ||
• Codes for a membrane bound protein that allows for the transport of L-carnitine into the cell. <br> | • Codes for a membrane bound protein that allows for the transport of L-carnitine into the cell. <br> | ||
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| - | <b> | + | <b>caiX</b> <br> |
• From <i>pseudomonas aeruginosa</i> strain PAO1<br> | • From <i>pseudomonas aeruginosa</i> strain PAO1<br> | ||
• Codes for a transport protein that allows for L-carnitine to be directed to the membrane bound channel to then be transported into the cell. <br> | • Codes for a transport protein that allows for L-carnitine to be directed to the membrane bound channel to then be transported into the cell. <br> | ||
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| - | <b> | + | <b>cbcX</b> <br> |
• From <i>pseudomonas aeruginosa</i> strain PAO1 <br> | • From <i>pseudomonas aeruginosa</i> strain PAO1 <br> | ||
• Codes for a transport protien that takes choline to a transport channel to increase rate of choline uptake. <br> | • Codes for a transport protien that takes choline to a transport channel to increase rate of choline uptake. <br> | ||
Revision as of 02:36, 28 September 2013
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Cardiobiotics Parts
Carnitine dehydrogenase (CDHcab) BBa_K1205000
• Derived from pseudomonas aeruginosa strain PAO1
• This gene codes for L-Carnitine Dehydrogenase, a protein that breaks down L-carnitine into 3-Dehydrocarnitine. This enzyme directs the degradation down a pathway that prevents the formation of trimethylamine. As previously mentioned trimethylamine has been known to cause cardiovascular disease. This new pathway ultimately leads to glycine which is a nature substance in the body. This enzyme is the centerpiece of our experiment.
Characterization:
• This part was characterized with an enzymatic assay.
cbcVW
• From pseudomonas aeruginosa strain PAO1
• Codes for a membrane bound protein that allows for the transport of L-carnitine into the cell.
• This is crucial to our project because if we want to implement this as a system we need the cell to have the ability to uptake an excess of L-carnitine.
• Proof of functionality: LCMS Assay
Characterization:
Proof of functionality: LCMS
caiX
• From pseudomonas aeruginosa strain PAO1
• Codes for a transport protein that allows for L-carnitine to be directed to the membrane bound channel to then be transported into the cell.
• This is crucial to our project because if we want to implement this as a system we need the cell to have the ability to uptake an excess of L-carnitine.
• Proof of functionality: LCMS Assay
Characterization:
Proof of functionality: LCMS
cbcX
• From pseudomonas aeruginosa strain PAO1
• Codes for a transport protien that takes choline to a transport channel to increase rate of choline uptake.
• This is useful to our project because choline is also a compound that can be degraded to TMA. If we also modified its degradation our probiotic would be even more effective in decreasing risk for CVD. This gene would help increase uptake to maximize our probiotic's effectiveness.
• Unfortunately, due to the constraints of time and money, this developed biobrick could not be characterized
