Sandbox Reserved 1559

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Function(s) and Biological Relevance

Lignostilbene-α,β-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. 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.

Broader Implications

Lignin represents 30% of the lignocellulose biomass. It consists of different aromatic building blocks, phenylpropanoids, which are extremely useful. Normally aromatic compounds are extracted from petroleum and are used to manufacture drugs, paint, plastics, etc. Therefore the potential of lignin is very high. Lignin is the most abundant polymer in nature other than cellulose and chitin, and it is the only one that contains such a large number of aromatic compounds.

Structural highlights and structure-function relationships

The of the consists of Phenylalanine59, Tyrosine101, and Lysine134.

The flat surface of the B-sheet is pushing the amino acids up, making it possible for the catalytic triad Phe59, Tyr101, and Lys134 to create interactions with the .

Energy Transformation

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