Sandbox Reserved 1559: Difference between revisions

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== Function(s) and Biological Relevance ==
== Function(s) and Biological Relevance ==
<scene name='82/823083/6ojt/1'>Lignostilbene-α,β-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009</scene> is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. LsdA has greatest substrate specificity for lignostilbene. The substrate's 4-hudryoxy moiety is required for catalysis. Phenylazophenol inhibits the cleavage of lignostilbene by LsdA. The breaking down of lignin is essential to the sustainable biorefining of lignocellulose. It is of great relevance to transforming lignocellulose to biofuels.<ref> PMID:31292192 </ref>
<scene name='82/823083/6ojt/1'>Lignostilbene-α,β-dioxygenase A (LsdA) from the bacterium ''Sphingomonas paucimobilis'' TMY1009</scene> is a nonheme iron oxygenase that catalyzes the cleavage of lignostilbene, a compound arising in lignin transformation, to two vanillin molecules. LsdA has greatest substrate specificity for lignostilbene. The substrate's 4-hydryoxy moiety is required for catalysis. Phenylazophenol inhibits the cleavage of lignostilbene by LsdA. The breaking down of lignin is essential to the sustainable biorefining of lignocellulose. It is of great relevance to transforming lignocellulose to biofuels.<ref> PMID:31292192 </ref>




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== Energy Transformation ==
== Energy Transformation ==
Phenylazophenol inhibits the LsdA-catalyzed cleavage of lignostilbene in a reversible, mixed fashion. <ref>PMID 31292192</ref>
Phenylazophenol inhibits the LsdA-catalyzed cleavage of lignostilbene in a reversible, mixed fashion.