Sandbox Reserved 1065
| 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. |
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General mechanism for the activation of fatty acidsFadD13 first activates the fatty acid through a reaction with ATP to form an acyl adenylate intermediate and release pyrophosphate. Following a conformational change of the enzyme, coenzyme A is able to bind and reaction with the acyl adenylate intermediate forming the acyl CoA product (Figure 1). active site (to be copied over)Mutational studies showed that high conserved residue in the C-terminal region, , 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.[1] Additionally, Serine 404 was hypothesized to be involved in the binding of Coenzyme A which may only occur once this region incurs a 140 degree rotational change.[2][1]
FunctionThis is the .[3] This is the .[3] FadD13 has three different : The N-terminal region (1-395) is in blue, the C-terminal region (402-403) is in red, and the six amino acid linker is in tan (citation for original paper). The adenine of ATP is bound to a group of that is structurally identically to other acyl-CoA synthetases (Citation for original paper). citation 1 [2] citation 2 [4] Citation 3 [5]
DiseaseRelevanceStructural highlightsThis 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.
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ReferencesReferences
- ↑ 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
- ↑ 2.0 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
- ↑ 3.0 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
- ↑ 4.0 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
- ↑ 5.0 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