Difference between revisions of "Part:BBa K1497018"
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src="https://static.igem.org/mediawiki/parts/1/16/F3H_Reaktion.jpg"></p> | src="https://static.igem.org/mediawiki/parts/1/16/F3H_Reaktion.jpg"></p> | ||
<br> | <br> | ||
− | <p class="MsoCaption" align="text-align:justify"><span lang="EN-US"><b>Figure | + | <p class="MsoCaption" align="text-align:justify"><span lang="EN-US"><b>Figure 2</b></span></a><span lang="EN-US"> |
Reaction of the F3H </span></p> | Reaction of the F3H </span></p> | ||
</td> | </td> | ||
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<partinfo>BBa_K1497018 parameters</partinfo> | <partinfo>BBa_K1497018 parameters</partinfo> | ||
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+ | ===References=== | ||
+ | |||
+ | 1. Petit P, Granier T, d’Estaintot BL, et al. (2007) Crystal structure of grape dihydroflavonol 4-reductase, a key enzyme in flavonoid biosynthesis. Journal of molecular biology 368:1345–57. doi: 10.1016/j.jmb.2007.02.088 | ||
+ | |||
+ | 2. Gollop R, Even S, Colova-tsolova V, et al. (2002) Expression of the grape dihydroflavonol reductase gene and analysis of its promoter region 1. 53:1397–1409. | ||
+ | |||
+ | 3. Liew C, Loh C, Goh C, Lim S (1998) The isolation , molecular characterization and expression of dihydroflavonol 4-reductase cDNA in the orchid , Bromheadia. 135:161–169. | ||
+ | |||
+ | 4. Tanaka Y, Brugliera F, B PTRS, et al. (2013) Flower colour and cytochromes P450 Flower colour and cytochromes P450. |
Revision as of 17:10, 17 October 2014
B0034-F3H-B0034-DFR
This part encodes the sequence for the enzyme Flavanone-3ß-hydroxylase (F3H) EC 1.2.7.3 from Petroselinum crispum. F3H catalyze naringenin, an anthocyanidin precursor, to the substance dihydroflavonol (Tanaka, 2006) and the dihydroflavonol 4-reductase.
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+ |
Figure 2 Reaction of the F3H |
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 185
Illegal BamHI site found at 675
Illegal BamHI site found at 1481 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1233
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 1218
References
1. Petit P, Granier T, d’Estaintot BL, et al. (2007) Crystal structure of grape dihydroflavonol 4-reductase, a key enzyme in flavonoid biosynthesis. Journal of molecular biology 368:1345–57. doi: 10.1016/j.jmb.2007.02.088
2. Gollop R, Even S, Colova-tsolova V, et al. (2002) Expression of the grape dihydroflavonol reductase gene and analysis of its promoter region 1. 53:1397–1409.
3. Liew C, Loh C, Goh C, Lim S (1998) The isolation , molecular characterization and expression of dihydroflavonol 4-reductase cDNA in the orchid , Bromheadia. 135:161–169.
4. Tanaka Y, Brugliera F, B PTRS, et al. (2013) Flower colour and cytochromes P450 Flower colour and cytochromes P450.