Sandbox Reserved 1065

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A high conserved residue in the C-terminal region,<scene name='69/694233/Lys_487/2'>Lys 487</scene>, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate.<ref name="residue paper">PMID: 20027301</ref> Other mutation studies, found that Serine 404 was involved in the binding of Coenzyme A which may only occur once the region incurs a 140 degree rotational change.<ref name="Our Paper"/><ref name="residue paper"/>
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A high conserved residue in the C-terminal region, <scene name='69/694233/Lys_487/2'>Lysine 487</scene>, resulted in a 95% loss of function of FadD13 and is thought to be involved in the orientation of the substrates to form the adenylate intermediate.<ref name="residue paper">PMID: 20027301</ref> Other mutation studies, found that Serine 404 was involved in the binding of Coenzyme A which may only occur once the region incurs a 140 degree rotational change.<ref name="Our Paper"/><ref name="residue paper"/>

Revision as of 01:15, 9 April 2015

This Sandbox is Reserved from 02/09/2015, through 05/31/2016 for use in the course "CH462: Biochemistry 2" taught by Geoffrey C. Hoops at the Butler University. This reservation includes Sandbox Reserved 1051 through Sandbox Reserved 1080.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing


Your Heading Here (maybe something like 'Structure')

Very Long Chain Fatty Acyl CoA Synthetase (FadD13)

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Khare G, Gupta V, Gupta RK, Gupta R, Bhat R, Tyagi AK. Dissecting the role of critical residues and substrate preference of a Fatty Acyl-CoA Synthetase (FadD13) of Mycobacterium tuberculosis. PLoS One. 2009 Dec 21;4(12):e8387. doi: 10.1371/journal.pone.0008387. PMID:20027301 doi:10.1371/journal.pone.0008387
  2. ↑ 2.0 2.1 Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012
  3. ↑ 3.0 3.1 3.2 Andersson CS, Lundgren CA, Magnusdottir A, Ge C, Wieslander A, Molina DM, Hogbom M. The Mycobacterium tuberculosis Very-Long-Chain Fatty Acyl-CoA Synthetase: Structural Basis for Housing Lipid Substrates Longer than the Enzyme. Structure. 2012 May 2. PMID:22560731 doi:10.1016/j.str.2012.03.012
  4. ↑ 4.0 4.1 Jatana N, Jangid S, Khare G, Tyagi AK, Latha N. Molecular modeling studies of Fatty acyl-CoA synthetase (FadD13) from Mycobacterium tuberculosis--a potential target for the development of antitubercular drugs. J Mol Model. 2011 Feb;17(2):301-13. doi: 10.1007/s00894-010-0727-3. Epub 2010 May, 8. PMID:20454815 doi:http://dx.doi.org/10.1007/s00894-010-0727-3
  5. ↑ 5.0 5.1 Schroeder EK, de Souza N, Santos DS, Blanchard JS, Basso LA. Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis. Curr Pharm Biotechnol. 2002 Sep;3(3):197-225. PMID:12164478
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