Difference between revisions of "Talk:Part:BBa K343001"
(New page: =Forslag til opbygning= =Beta-carotene dioxygenase= β,β-carotene-15,15′-dioxygenase is an enzyme that cleaves beta-carotene into two retinal, via the following reaction: Beta-caroten...) |
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| + | - Et bedre navn under Hard info | ||
| + | - Usage and parameters sektion | ||
=Beta-carotene dioxygenase= | =Beta-carotene dioxygenase= | ||
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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). | 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). | + | 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). |
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| + | Here we present a biobrick containing this enzyme, and show that it produces retinal both when beta-caroton is added directly to the bacteria or in bacteria with the Cambridge 2009 BBa_K274210 (CrtEBIY under constitutive promoter) BioBrick (4) which produces beta-caroten ''in vivo''. | ||
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| + | ==Background== | ||
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| + | 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). | ||
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| + | 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). | ||
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| + | 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. | ||
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==Usage and parameters sektion== | ==Usage and parameters sektion== | ||
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3. http://en.wikipedia.org/wiki/Retinal | 3. http://en.wikipedia.org/wiki/Retinal | ||
4. https://parts.igem.org/Part:BBa_K274210 | 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 | ||
Revision as of 07:44, 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 the bacteria or in bacteria with 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.
Usage and parameters sektion
Characterization sektion
Risk-assesment
Litterature
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