Difference between revisions of "Part:BBa K3633011"
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<partinfo>BBa_K3633011 short</partinfo> | <partinfo>BBa_K3633011 short</partinfo> | ||
| − | Betalains are water-soluble nitrogen-containing pigments that are subdivided | + | ==Description== |
| + | |||
| + | Betalains are water-soluble nitrogen-containing pigments that are subdivided in red-violet betacyanins and yellow-orange betaxanthins. Due to glycosylation and acylation betalains exhibit a huge structural diversity. Betanin (betanidin-5-O--glucoside) is the most common betacyanin in the plant kingdom. | ||
The biosynthesis of betalains in plants excludes that of anthocyanins. During the biosynthesis of betalains in the cytoplasm three enzymes are involved: Tyrosinase, 4,5-DOPA-extradioldioxygenase, and betanidin-glucosyltransferase. The amino acid L-tyrosine, which is enzymatically formed over the shikimate pathway from arogenic acid, is the precursor for the biosynthesis of L-DOPA. Tyrosine is hydroxylated by means of the enzyme tyrosinase to DOPA (I) that is formed to betalamic acid or to cyclo-DOPA. The biosynthesis of betalamic acid, which is the basic structure of betalains as follow: 4,5-DOPA-extradiol dioxygenase opens the cyclic ring of L-DOPA between carbons 4 and 5, thus producing 4,5-seco-DOPA (II). This intermediate product occurs naturally. Due to spontaneous intramolecular condensation between the amine group and the aldehyde group of 4,5-seco-DOPA betalamic acid is formed. | The biosynthesis of betalains in plants excludes that of anthocyanins. During the biosynthesis of betalains in the cytoplasm three enzymes are involved: Tyrosinase, 4,5-DOPA-extradioldioxygenase, and betanidin-glucosyltransferase. The amino acid L-tyrosine, which is enzymatically formed over the shikimate pathway from arogenic acid, is the precursor for the biosynthesis of L-DOPA. Tyrosine is hydroxylated by means of the enzyme tyrosinase to DOPA (I) that is formed to betalamic acid or to cyclo-DOPA. The biosynthesis of betalamic acid, which is the basic structure of betalains as follow: 4,5-DOPA-extradiol dioxygenase opens the cyclic ring of L-DOPA between carbons 4 and 5, thus producing 4,5-seco-DOPA (II). This intermediate product occurs naturally. Due to spontaneous intramolecular condensation between the amine group and the aldehyde group of 4,5-seco-DOPA betalamic acid is formed. | ||
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| − | + | ==Experiments & Results== | |
| − | == | + | |
| − | + | ==Sequence & Features== | |
| − | <span class='h3bb'> | + | <span class='h3bb'></span> |
<partinfo>BBa_K3633011 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3633011 SequenceAndFeatures</partinfo> | ||
Revision as of 05:46, 24 October 2020
A composite part to express 4,5-DODA, responsible for production of betalains
Description
Betalains are water-soluble nitrogen-containing pigments that are subdivided in red-violet betacyanins and yellow-orange betaxanthins. Due to glycosylation and acylation betalains exhibit a huge structural diversity. Betanin (betanidin-5-O--glucoside) is the most common betacyanin in the plant kingdom.
The biosynthesis of betalains in plants excludes that of anthocyanins. During the biosynthesis of betalains in the cytoplasm three enzymes are involved: Tyrosinase, 4,5-DOPA-extradioldioxygenase, and betanidin-glucosyltransferase. The amino acid L-tyrosine, which is enzymatically formed over the shikimate pathway from arogenic acid, is the precursor for the biosynthesis of L-DOPA. Tyrosine is hydroxylated by means of the enzyme tyrosinase to DOPA (I) that is formed to betalamic acid or to cyclo-DOPA. The biosynthesis of betalamic acid, which is the basic structure of betalains as follow: 4,5-DOPA-extradiol dioxygenase opens the cyclic ring of L-DOPA between carbons 4 and 5, thus producing 4,5-seco-DOPA (II). This intermediate product occurs naturally. Due to spontaneous intramolecular condensation between the amine group and the aldehyde group of 4,5-seco-DOPA betalamic acid is formed.
In order to make the production of the Betacyanin much efficient, Shanghai_SFLS_SPBS successfully change the RBS and makes it express in the E.coli and Vibrio natriegens.
Experiments & Results
Sequence & Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 7
Illegal NheI site found at 30 - 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]