Sandbox Reserved 1643
From Proteopedia
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
| - | == Structure == | + | == '''Structure''' == |
| - | == Function == | + | == '''Function''' == |
| - | == Applications== | + | == '''Applications''' == |
| - | *Mutation of PET hydrolase | + | *'''Mutation of PET hydrolase''' |
Today 349 putative PET hydrolases are identified in marine and terrestrial datasets. These PET hydrolase frequencies ranged from 0.004 to 0.92 hits/Mb and 0.0001 to 1.513 hits/Mb for marine and terrestrial datasets, respectively.[1] However, a metagenomic sample from a crude oil reservoir offered the highest rate of sequence hits, with a frequency about 1.5 hits/Mb.[1,2] | Today 349 putative PET hydrolases are identified in marine and terrestrial datasets. These PET hydrolase frequencies ranged from 0.004 to 0.92 hits/Mb and 0.0001 to 1.513 hits/Mb for marine and terrestrial datasets, respectively.[1] However, a metagenomic sample from a crude oil reservoir offered the highest rate of sequence hits, with a frequency about 1.5 hits/Mb.[1,2] | ||
Revision as of 20:54, 11 January 2021
| This Sandbox is Reserved from 26/11/2020, through 26/11/2021 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1643 through Sandbox Reserved 1664. |
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PET Hydrolase
One of the biggest problems in the world is the recycling of plastic. The stability of the polymers, their crystallinity and their hydrophilic surface make recycling difficult. Polyethylene terephthalate PET is one of the most widely used plastics today (around 30 million tons per year) and its recycling is now possible thanks to PET hydrolase, an enzyme isolated from the bacteria Ideonella sakaiensis. [1]
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
