Sandbox Reserved 987
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. | ||
| - | == | + | == Background == |
| - | Cocaine Esterase (CocE) is the most efficient protein to hydrolyze the cocaine domain known to date ''in vivo''.<sup><ref>"Effects of cocaine esterase following its repeated administration with cocaine in mice" Mei-Chaun Ko, Diwahar Narasimhan, Aaron A. Berlin, Nicholas W. Lukacs, Roger K. Sunahara, James H. Woods. Drug and Alcohol Dependence 1 May 2009;101:202-09. doi: 10.1016/j.drugalcdep.2009.01.002</ref></sup> Cocaine Esterase is used in bacterium ''Rhodococcus'' which hydrolyzes the cocaine that it uptakes and uses it for carbons and nitrogens. Although this protein metabolizes cocaine in bacterium, it is sure to induce an immune response as it is foreign to the human body. This could mitigate the effects of CocE if a person had suffered from cocaine toxicity. | + | Cocaine Esterase (CocE) is the most efficient protein to hydrolyze the cocaine domain known to date ''in vivo''.<sup><ref>"Effects of cocaine esterase following its repeated administration with cocaine in mice" Mei-Chaun Ko, Diwahar Narasimhan, Aaron A. Berlin, Nicholas W. Lukacs, Roger K. Sunahara, James H. Woods. Drug and Alcohol Dependence 1 May 2009;101:202-09. doi: 10.1016/j.drugalcdep.2009.01.002</ref></sup> Cocaine Esterase is used in bacterium ''Rhodococcus'' which hydrolyzes the cocaine that it uptakes and uses it for carbons and nitrogens. Although this protein metabolizes cocaine in bacterium, it is sure to induce an immune response as it is foreign to the human body. This could mitigate the effects of CocE if a person had suffered from cocaine toxicity. |
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== Structure == | == Structure == | ||
<scene name='69/691529/Cocaine_esterase/1'>TextToBeDisplayed</scene> | <scene name='69/691529/Cocaine_esterase/1'>TextToBeDisplayed</scene> | ||
| - | == | + | |
| + | == Function == | ||
Cocaine esterase is used to catalyze the following reaction: | Cocaine esterase is used to catalyze the following reaction: | ||
cocaine + H<sub>2</sub>O ←→ ecgonine methyl ester + benzoate <sup><ref>Cocaine esterase | cocaine + H<sub>2</sub>O ←→ ecgonine methyl ester + benzoate <sup><ref>Cocaine esterase | ||
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Reaction mechanism for cocaine esterase-catalyzed hydrolyses of (+)- and (-)-cocaine: unexpected common rate-determining step. | Reaction mechanism for cocaine esterase-catalyzed hydrolyses of (+)- and (-)-cocaine: unexpected common rate-determining step. | ||
Liu J1, Zhao X, Yang W, Zhan CG. | Liu J1, Zhao X, Yang W, Zhan CG. | ||
| - | == | + | |
| + | == Medical Relevance == | ||
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
Revision as of 20:25, 24 February 2015
| This Sandbox is Reserved from 20/01/2015, through 30/04/2016 for use in the course "CHM 463" taught by Mary Karpen at the Grand Valley State University. This reservation includes Sandbox Reserved 987 through Sandbox Reserved 996. |
To get started:
More help: Help:Editing |
Contents |
Cocaine Esterase
|
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Background
Cocaine Esterase (CocE) is the most efficient protein to hydrolyze the cocaine domain known to date in vivo.[3] Cocaine Esterase is used in bacterium Rhodococcus which hydrolyzes the cocaine that it uptakes and uses it for carbons and nitrogens. Although this protein metabolizes cocaine in bacterium, it is sure to induce an immune response as it is foreign to the human body. This could mitigate the effects of CocE if a person had suffered from cocaine toxicity.
Structure
Function
Cocaine esterase is used to catalyze the following reaction: cocaine + H2O ←→ ecgonine methyl ester + benzoate [4] Reaction mechanism for cocaine esterase-catalyzed hydrolyses of (+)- and (-)-cocaine: unexpected common rate-determining step. Liu J1, Zhao X, Yang W, Zhan CG.
Medical Relevance
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
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
- ↑ "Effects of cocaine esterase following its repeated administration with cocaine in mice" Mei-Chaun Ko, Diwahar Narasimhan, Aaron A. Berlin, Nicholas W. Lukacs, Roger K. Sunahara, James H. Woods. Drug and Alcohol Dependence 1 May 2009;101:202-09. doi: 10.1016/j.drugalcdep.2009.01.002
- ↑ Cocaine esterase From Wikipedia, the free encyclopedia
