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Team:Wageningen UR/Lovastatin
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<p>As an inhibitor of the enzyme (3-hydroxy-3-methylglutaryl CoA reductase), which plays a significant role in cholesterol biosynthesis, lovastatin is a medicinal compound used against cardiovascular diseases (Tobert, 2003). It is a naturally occurring drug which is found in food such as oyster mushrooms and red yeast rice. During the production of lovastatin in Aspergillus terreus, toxins could be produced at the same time. However, Aspergillus niger is a mass producer of organic acids with the potential to produce lovastatin more securely. By this project, a more suitable host for lovastatin biosynthesis is likely to be found by cloning and transferring the gene from Aspergillus terreus to the same species fungi Aspergillus niger.</p> | <p>As an inhibitor of the enzyme (3-hydroxy-3-methylglutaryl CoA reductase), which plays a significant role in cholesterol biosynthesis, lovastatin is a medicinal compound used against cardiovascular diseases (Tobert, 2003). It is a naturally occurring drug which is found in food such as oyster mushrooms and red yeast rice. During the production of lovastatin in Aspergillus terreus, toxins could be produced at the same time. However, Aspergillus niger is a mass producer of organic acids with the potential to produce lovastatin more securely. By this project, a more suitable host for lovastatin biosynthesis is likely to be found by cloning and transferring the gene from Aspergillus terreus to the same species fungi Aspergillus niger.</p> | ||
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| + | == Reference == | ||
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| + | <span id="ref1" class="ref">1.</span>Alieva, N.O., et al., Diversity and evolution of coral fluorescent proteins. Plos One, 2008. 3(7): p. e2680.<br/> | ||
| + | <span id="ref2" class="ref">2.</span>Chan, M.C., et al., Structural characterization of a blue chromoprotein and its yellow mutant from the sea anemone Cnidopus japonicus. Journal of Biological Chemistry, 2006. 281(49): p. 37813-37819.<br/> | ||
| + | <span id="ref3" class="ref">3.</span>Shagin, D.A., et al., GFP-like proteins as ubiquitous metazoan superfamily: evolution of functional features and structural complexity. Molecular biology and evolution, 2004. 21(5): p. 841-850.<br/> | ||
| + | <span id="ref4" class="ref">4.</span>Prescott, M., et al., The 2.2 Å crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation. Structure, 2003. 11(3): p. 275-284.<br/> | ||
| + | <span id="ref5" class="ref">5.</span>Shkrob, M., et al., Far-red fluorescent proteins evolved from a blue chromoprotein from Actinia equina. Biochem. J, 2005. 392: p. 649-654.<br/> | ||
| + | <span id="ref6" class="ref">6.</span>Chalfie, M. and S.R. Kain, Methods of Biochemical Analysis, Green Fluorescent Protein: Properties, Applications and Protocols2005: Wiley-Liss.<br/> | ||
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Revision as of 09:18, 16 September 2013
- Safety introduction
- General safety
- Fungi-related safety
- Biosafety Regulation
- Safety Improvement Suggestions
- Safety of the Application
Lovastatin
All you need is lov.
Introduction
As an inhibitor of the enzyme (3-hydroxy-3-methylglutaryl CoA reductase), which plays a significant role in cholesterol biosynthesis, lovastatin is a medicinal compound used against cardiovascular diseases (Tobert, 2003). It is a naturally occurring drug which is found in food such as oyster mushrooms and red yeast rice. During the production of lovastatin in Aspergillus terreus, toxins could be produced at the same time. However, Aspergillus niger is a mass producer of organic acids with the potential to produce lovastatin more securely. By this project, a more suitable host for lovastatin biosynthesis is likely to be found by cloning and transferring the gene from Aspergillus terreus to the same species fungi Aspergillus niger.
== Reference ==
1.Alieva, N.O., et al., Diversity and evolution of coral fluorescent proteins. Plos One, 2008. 3(7): p. e2680.
2.Chan, M.C., et al., Structural characterization of a blue chromoprotein and its yellow mutant from the sea anemone Cnidopus japonicus. Journal of Biological Chemistry, 2006. 281(49): p. 37813-37819.
3.Shagin, D.A., et al., GFP-like proteins as ubiquitous metazoan superfamily: evolution of functional features and structural complexity. Molecular biology and evolution, 2004. 21(5): p. 841-850.
4.Prescott, M., et al., The 2.2 Å crystal structure of a pocilloporin pigment reveals a nonplanar chromophore conformation. Structure, 2003. 11(3): p. 275-284.
5.Shkrob, M., et al., Far-red fluorescent proteins evolved from a blue chromoprotein from Actinia equina. Biochem. J, 2005. 392: p. 649-654.
6.Chalfie, M. and S.R. Kain, Methods of Biochemical Analysis, Green Fluorescent Protein: Properties, Applications and Protocols2005: Wiley-Liss.
