Sandbox Reserved 1558

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== Function(s) and Biological Relevance ==
== Function(s) and Biological Relevance ==
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Lignostilbene-α,β-dioxygenase (LsdA) from the bacterium
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Lignostilbene-α,β-dioxygenase (LsdA) from the bacterium ''''Sphingomonas paucimobilis''''. It is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound
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''''Sphingomonas paucimobilis''''. It is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound
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arising in lignin transformation, to two vanillin molecules. The substrate for this enzyme is lignostilbene. Phenylazophenol inhibited the LsdA-catalyzed cleavage of lignostilbene in a reversible, mixed fashion. Lignin is used in biofuel production. Lignin is a heterogeneous aromatic polymer found in plant cell walls that contributes to the recalcitrance of biomass. Below are two images. On the left is Lignostilbene, and on the right is Vanillin for comparison.
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arising in lignin transformation, to two vanillin molecules. The substrate for this enzyme is lignostilbene. Phenylazophenol
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inhibited the LsdA-catalyzed cleavage of lignostilbene in a
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reversible, mixed fashion. Lignin is used in biofuel production. Lignin is a heterogeneous aromatic polymer found in plant
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cell walls that contributes to the recalcitrance of biomass. Below are two images. On the left is Lignostilbene, and on the right is Vanillin for comparison.
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[[Image:lignostilbene.png]][[Image:vanillin.png]]
[[Image:lignostilbene.png]][[Image:vanillin.png]]
== Broader Implications ==
== Broader Implications ==
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To examine LsdA’s substrate specificity, we heterologously produce the dimeric enzyme with the help of chaperones. When
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To examine LsdA’s substrate specificity, we heterologously produce the dimeric enzyme with the help of chaperones. When tested on several substituted stilbenes, LsdA exhibited the greatest specificity for lignostilbene. These experiments further indicate that the substrate’s
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tested on several substituted stilbenes, LsdA exhibited the greatest specificity for lignostilbene. These experiments further indicate that the substrate’s
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4-hydroxy moiety is required for catalysis and that this moiety
4-hydroxy moiety is required for catalysis and that this moiety
cannot be replaced with a methoxy group. This expands our
cannot be replaced with a methoxy group. This expands our

Revision as of 01:49, 9 December 2019

This Sandbox is Reserved from Aug 26 through Dec 12, 2019 for use in the course CHEM 351 Biochemistry taught by Bonnie_Hall at the Grand View University, Des Moines, USA. This reservation includes Sandbox Reserved 1556 through Sandbox Reserved 1575.
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Lignostilbene-α,β-dioxygenase A (LsdA) Catalyzation

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References

Kuatsjah, Eugene, et al. “Identification of Functionally Important Residues and Structural Features in a Bacterial Lignostilbene Dioxygenase.” Journal of Biological Chemistry, vol. 294, no. 35, 2019, pp. 12911–12920., doi:10.1074/jbc.ra119.009428.

  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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