Sandbox Reserved 1568: Difference between revisions
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== Function(s) and Biological Relevance == | == Function(s) and Biological Relevance == | ||
Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). | Lignostilbene-α,ß-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009 is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules (see images below). Lignin is a common component of biomass that scientists are interested in finding ways to break down to simpler and useful materials. | ||
[[Image:lignostilbene.png]][[Image:Vanillin.png]] | [[Image:lignostilbene.png]][[Image:Vanillin.png]] | ||
Revision as of 16:42, 29 November 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,ß-dioxygenase A (LsdA) structure and function
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