From 2008.igem.org
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- | *4-coumarate CoA ligase :: Stilbene synthase fusion protein (4CL:STS) - Completes the resveratrol biosynthetic pathwy by catalyzing the conversion of ''p''-coumaric acid to resveratrol, with a stoichiometry of 2:1. | + | *4-coumarate CoA ligase :: Stilbene synthase fusion protein (4CL:STS) - Completes the resveratrol biosynthetic pathway by catalyzing the conversion of ''p''-coumaric acid to resveratrol, with a stoichiometry of 2:1. The 4CL:STS fusion protein was selected because it has been shown to more efficiently produce resveratrol than coexpression of the proteins separately (possibly due to substrate channeling). |
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Revision as of 17:15, 29 October 2008
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SUMMARY ::: BACKGROUND ::: STRATEGY ::: CONSTRUCTS ::: RESULTS ::: ONGOING WORK ::: OUR TEAM ::: NOTEBOOK ::: GALLERY
Metabolic Parts
- Tyrosine Ammonia Lyase (TAL) - Begins the resveratrol biosynthetic pathway by catalyzing the the conversion of L-tyrosine to ammonia and p-coumaric acid. TAL also has activity as Phenylalanine Ammonia Lyase (PAL) via conversion of L-phenylalanine to ammonia and trans-cinnamic acid. The Rhodotorula glutinis TAL was selected specifically because of its relatively high TAL/PAL activity ratio, and its successful expression in Saccharomyces cerevisiae and Escherichia coli. The p-coumaric acid produced by TAL will later be converted to resveratrol, while the trans-cinnamic acid will add a "floral" and "honey-like" bouquet to the beer.
- 4-coumarate CoA ligase :: Stilbene synthase fusion protein (4CL:STS) - Completes the resveratrol biosynthetic pathway by catalyzing the conversion of p-coumaric acid to resveratrol, with a stoichiometry of 2:1. The 4CL:STS fusion protein was selected because it has been shown to more efficiently produce resveratrol than coexpression of the proteins separately (possibly due to substrate channeling).
Circuit Design
Cellular Chassis
Fermentation Apparatus
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SUMMARY ::: BACKGROUND ::: STRATEGY ::: CONSTRUCTS ::: RESULTS ::: ONGOING WORK ::: OUR TEAM ::: NOTEBOOK ::: GALLERY
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