Sandbox Reserved 1558

From Proteopedia

(Difference between revisions)

Revision as of 00:54, 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.

To get started:

Click the edit this page tab at the top. Save the page after each step, then edit it again.
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

Lignostilbene-α,β-dioxygenase A (LsdA) Catalyzation

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.

You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

1 Function(s) and Biological Relevance
2 Broader Implications
3 Structural highlights and structure-function relationships
4 Energy Transformation

Function(s) and Biological Relevance

Lignostilbene-,-dioxygenase A (LsdA) from the bacterium 'Sphingomonas paucimobilis'. It is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound 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.

Broader Implications

To examine LsdA’s substrate specificity, we heterologously produced the dimeric enzyme with the help of chaperones. When tested on several substituted stilbenes, LsdA exhibited the greatest specificity for lignostilbene. These experiments further indicated that the substrate’s 4-hydroxy moiety is required for catalysis and that this moiety cannot be replaced with a methoxy group. This study expands our mechanistic understanding of LsdA and related stilbene-cleaving dioxygenases.

Structural highlights and structure-function relationships

The is a fold of LsdA of a seven-bladed -propeller, typical of the CCOs.

The and space-filling view of the ligand in the protein, shows that both hydrophilic and hydrophobic residues are important to the ligand in the binding site.

Energy Transformation

Phenylazophenol inhibits the LsdA-catalyzed cleavage of lignostilbene in a reversible, mixed fashion.

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.

↑ 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
↑ 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

Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Reserved_1558"

Sandbox Reserved 1558

From Proteopedia

Revision as of 00:54, 9 December 2019

Lignostilbene-α,β-dioxygenase A (LsdA) Catalyzation

Contents

Function(s) and Biological Relevance

Broader Implications

Structural highlights and structure-function relationships

Energy Transformation

References

Views

Personal tools

Navigation

Search

Toolbox

@@ Line 11: / Line 11: @@
 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
+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.
 [[Image:lignostilbene.png]][[Image:vanillin.png]]