Difference between revisions of "Talk:Part:BBa K343001"
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[[Image:SDU-Denmark-2010-retinal-synthesis.gif|200px|thumb|right|Retinal synthesis pathway]] | [[Image:SDU-Denmark-2010-retinal-synthesis.gif|200px|thumb|right|Retinal synthesis pathway]] | ||
| − | β,β-carotene-15,15′-dioxygenase is an enzyme that cleaves beta-carotene into two retinal, via the following reaction: Beta-carotene + O(2) <=> 2 retinal <ref> | + | β,β-carotene-15,15′-dioxygenase is an enzyme that cleaves beta-carotene into two retinal, via the following reaction: Beta-carotene + O(2) <=> 2 retinal <ref>Test</ref>. |
Beta-carotene dioxygenase plays an important role in animal vision, as retinal forms the chemical basis for vision in animals (2). Animals cannot synthesize retinal ''de novo'' and thus relies on beta-carotene dioxygenase to transform carotenoids (beta-carotene, alpha-carotene, gamma-carotene, and beta-cryptoxanthin) into retinal (3). | Beta-carotene dioxygenase plays an important role in animal vision, as retinal forms the chemical basis for vision in animals (2). Animals cannot synthesize retinal ''de novo'' and thus relies on beta-carotene dioxygenase to transform carotenoids (beta-carotene, alpha-carotene, gamma-carotene, and beta-cryptoxanthin) into retinal (3). | ||
Revision as of 09:03, 13 October 2010
Contents
Mangler
- Et bedre navn under Hard info
- Usage and parameters sektion
Beta-carotene dioxygenase
β,β-carotene-15,15′-dioxygenase is an enzyme that cleaves beta-carotene into two retinal, via the following reaction: Beta-carotene + O(2) <=> 2 retinal [1].
Beta-carotene dioxygenase plays an important role in animal vision, as retinal forms the chemical basis for vision in animals (2). Animals cannot synthesize retinal de novo and thus relies on beta-carotene dioxygenase to transform carotenoids (beta-carotene, alpha-carotene, gamma-carotene, and beta-cryptoxanthin) into retinal (3).
Here we present a biobrick containing this enzyme, and show that it produces retinal both when beta-caroton is added directly to a bacteria containing this BioBrick; and in bacteria double transformated with this BioBrick and the Cambridge 2009 BBa_K274210 (CrtEBIY under constitutive promoter) BioBrick (4) which produces beta-caroten in vivo.
Background
Only two mechanisms for collecting light energy and converting it into chemical energy have been found in nature so fare. The first mechanism is dependent upon photochemical reaction centers (a multisubunit protein complex containing chlorophylls or bacteriochlorophylls, in which light energy is transduced into redox chemistry). The second mechanism uses rhodopsins, retinal-binding proteins that respond to light stimuli (5).
The later mechanism is found extensively througout nature, which has been speculated to be because of the ease, with which this system works; lateral transfer of rhodopsin-based photosystems requires only the genes encoding the rhodopsin apoprotein and a carotenoid oxygenase that produces retinal (5).
The use of rhodopsin photosystes could be of great use in synthetic biology, but this also requires a retinal-forming brick, which we present here.
Retinal
Retinal (also called retinaldehyde, vitamin A aldehyde or RAL) has the molecular formular C20H28O and weighs 284.43572 [g/mol]. C 84.45%, H 9.92%, O 5.63%. Melting point at 61-64 degrees celcius. The molecule can exist in four stereoisomeric forms (6).
The apperence of the molecule is orange crystals (in petr ether). UV max is 373 nm (in cyclohexane). Soluble in ethanol, chloroform, cyclohexane, petr ether and oils (6).
Beta-carotene dioxygenase gene from Drosophila melanogaster
The beta-carotene dioxygenase gene (also called "neither inactivation nor afterpotential B" or NinaB for short) was cloned from Drosophila melanogaster cDNA (7). This gene was the first beta-carotene dioxygenase to be molecularly identified and has been intensively studied (8).
Usage and parameters sektion
Characterization sektion
Risk-assesment
References
- ↑ Test
1. http://www.expasy.org/cgi-bin/nicezyme.pl?1.14.99.36 2. http://www.pnas.org/content/98/3/1130.full 3. http://en.wikipedia.org/wiki/Retinal 4. https://parts.igem.org/Part:BBa_K274210 5. http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TD0-4KYY3ND-1&_user=644074&_coverDate=11%2F30%2F2006&_rdoc=1&_fmt=high&_orig=search&_origin=search&_sort=d&_docanchor=&view=c&_searchStrId=1495939627&_rerunOrigin=scholar.google&_acct=C000034658&_version=1&_urlVersion=0&_userid=644074&md5=3e0c87176df546dc19016bf40977b03a&searchtype=a 6. http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi?cid=1070 7. http://www.ncbi.nlm.nih.gov/gene/41678 8. http://www.jbc.org/content/275/16/11915.long