Sandbox Reserved 1467

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== Function ==
== Function ==
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Two enzymes are responsible for the oxalate that is produced in the Burkholderia species. The first enzyme, ObcA, catalyzes the formation of a tetrahedral C6-CoA adduct from the substrates acetyl-COA and oxaloacetate. The second enzyme, ObcB, produces three products from the C6-CoA adduct. These products are oxalate, acetoacetate and CoA. The oxalate produced from the Burkholderia species, is necessary for bacterial growth and maintaining environmental pH.
== Disease ==
== Disease ==
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Species of Burkholderia can be involved in plant or human pathogenesis. Several diseases, such as ''B. Glumae'' which causes bacterial panicle blight in rice, or'' B. cepacia,'' which is an opportunistic pathogen in immunocompromised individuals, like those with cystic fibrosis or chronic granulomatous disease. It can also be involved with ''B. pseudomallei'' which can cause meliondosis, a lethal infection that leads to the formation of abscesses in internal organs.
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== Relevance ==
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== Relevance ==
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By studying the two mono-functional enzymes, ObcA and ObcB, there is a better understanding of the underlying molecular basis. . A bifunctional enzyme, Obc 1, can be used here for oxalogenesis. Researching and finding out more about these enzymes can help advance knowledge and potentially develop ways to control diseases associated with the ''Burkholderia'' species.
== Structural highlights ==
== Structural highlights ==

Revision as of 15:53, 14 November 2018

This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470.
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References

  1. 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
  2. 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
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