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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.
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
Energy Transformation
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