Difference between revisions of "Part:BBa K1497010"
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The dihydroflavonol 4-reductase (DFR; EC 1.1.1.219) from the plant <i> Dianthus caryophyllus </i> is an enzyme, catalyzing the reversible conversion of dihydroflavonols e.g. dihydro-kaempferol or dihydroquercetin into their corresponding leucoanthocyanidin. This reaction is NADPH-dependent (Liew et al. 1998) but its counter reaction can also occur with NAD<sub>+</sub> instead of NADP<sub>+</sub> (Queen Mary University of London 2014). DFR contains 353 amino acids and has a molecular weight of approximately 39.4 kDa. <br> <br>
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The dihydroflavonol 4-reductase (DFR; EC 1.1.1.219) from the plant <i> Dianthus caryophyllus </i> is an enzyme, catalyzing the reversible conversion of dihydroflavonols e.g. dihydro-kaempferol or dihydroquercetin into their corresponding leucoanthocyanidin. This reaction is NADPH-dependent (Liew et al. 1998) but its counter reaction can also occur with NAD<sub>+</sub> instead of NADP<sub>+</sub> (Queen Mary University of London 2014). DFR contains 353 amino acids and has a molecular weight of approximately 39.4 kDa. <br> <br>  
 
The iGEM Team TU Darmstadt 2014 used the DFR in combination with the <a href="/Part:BBa_K1497023">B0034</a>-RBS  and verified the function of the DFR in their pelargonidin operon <a href="/Part:BBa_K1497023">(K1497023)</a>.  
 
The iGEM Team TU Darmstadt 2014 used the DFR in combination with the <a href="/Part:BBa_K1497023">B0034</a>-RBS  and verified the function of the DFR in their pelargonidin operon <a href="/Part:BBa_K1497023">(K1497023)</a>.  
 
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====References====
 
====References====
  
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Chye-Fong Liew, Chiang-Shiomg Loh, Chong-Jin Goh, Saw-Hoon Lim 1998, 'The isolation, molecular characterization and expression of dihydroflavonol 4-reductase cDNA in the orchid, Bromheadia finlaysoniana', Plant Science,  vol. 135, no. 2, pp. 161-169. Available from: ScienceDirect (31.08.2014)<br>
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Chye-Fong Liew, Chiang-Shiomg Loh, Chong-Jin Goh, Saw-Hoon Lim 1998, 'The isolation, molecular characterization and expression of dihydroflavonol 4-reductase cDNA in the orchid, Bromheadia finlaysoniana', Plant Science,  vol. 135, no. 2, pp. 161-169. Available from: ScienceDirect (31.08.2014)<br> <br>
 
Queen Mary University of London, EC 1.1.1.219. Available from: <http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/1/1/219.html> (31.08.2014)
 
Queen Mary University of London, EC 1.1.1.219. Available from: <http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/1/1/219.html> (31.08.2014)

Revision as of 16:37, 11 October 2014

Dihydroflavonol 4-reductase (DFR)


The dihydroflavonol 4-reductase (DFR; EC 1.1.1.219) from the plant Dianthus caryophyllus is an enzyme, catalyzing the reversible conversion of dihydroflavonols e.g. dihydro-kaempferol or dihydroquercetin into their corresponding leucoanthocyanidin. This reaction is NADPH-dependent (Liew et al. 1998) but its counter reaction can also occur with NAD+ instead of NADP+ (Queen Mary University of London 2014). DFR contains 353 amino acids and has a molecular weight of approximately 39.4 kDa.

The iGEM Team TU Darmstadt 2014 used the DFR in combination with the B0034-RBS and verified the function of the DFR in their pelargonidin operon (K1497023).

Figure 1 Reaction of the DFR. One Dihydroflavonol reacts with NADPH to form a leucoanthocyanidin. The reverse reaction works with NAD+ or NADP+.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 330
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 82
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 67


References

Chye-Fong Liew, Chiang-Shiomg Loh, Chong-Jin Goh, Saw-Hoon Lim 1998, 'The isolation, molecular characterization and expression of dihydroflavonol 4-reductase cDNA in the orchid, Bromheadia finlaysoniana', Plant Science,  vol. 135, no. 2, pp. 161-169. Available from: ScienceDirect (31.08.2014)

Queen Mary University of London, EC 1.1.1.219. Available from: <http://www.chem.qmul.ac.uk/iubmb/enzyme/EC1/1/1/219.html> (31.08.2014)