Sandbox Reserved 1690

From Proteopedia

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== Function of your protein ==
== Function of your protein ==
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This is a picture of my protein with The Ligand highlighted as shown.
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This is a picture of my protein with The Ligand highlighted as shown. Our protein’s main function is to degrade GA and can be found in Fusarium oxysporum, a phytopathogenic fungus that uses GA as the sole carbon source for growth. It “hydrolyzes the glycosidic linkages of α-L-
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rhamnose-(1→4)-D-glucuronic acid (Rha–GlcA) present in GA side chains to release Rha through
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an anomer-retaining mechanism” (Kondo).
== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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Understanding the function and mechanism of this protein will allow us to create a solid foundation in the future for carbohydrate-related enzymes. This can eventually lead to using this enzyme's mechanism and target for medicinal advancement to help treat Batten's disease, which can cause death from the inability to excrete waste from the body via the form of lipids and proteins. The information obtained by this study associated with it will tell us more about the metabolic activity of the enzyme, which will allow us to use its properties for "elucidating its physiological function in plants" (Kondo)
== Important amino acids==
== Important amino acids==

Revision as of 15:28, 9 December 2021

This Sandbox is Reserved from 10/01/2021 through 01/01//2022 for use in Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1690 through Sandbox Reserved 1699.
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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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