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spinqualitylabelsall models Crystal Structure of Sphingomonas paucimobilis apo-LsdA Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Lignostilbene-α,β-dioxygenase A (LsdA) is a catalytic enzyme found in bacteria to break down cellulose components.

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Contents 1 Function 1.1 Lignostilbene 1.2 Vanillin 1.3 Cleavage of Lignostilbene 2 Broader Implications 3 Energy Transformation 4 Structural highlights

Function

Lignostilbene-α,β-dioxygenase A (LsdA) is an enzyme found in the bacteria Sphingomonas paucimbilis.^[1] It is used to catalyze the substrate, lignostilbene, into two vanillin molecules. Vanillin is a member of the benzaldehydes class and plays a role in the plant metabolite^[2]. Lignin is found in the plant cell walls, lignocellulose, and it gives the plant its rigid structure. The depolymerization of the lignin can allow for better use of the plants resources as a source of biofuel.

Lignostilbene

The lignostilbene is a compound found in cellulose

Vanillin

Vanillin is the product from the cleavage of lignostilbene from LsdA.

Cleavage of Lignostilbene

Broader Implications

Lignocellulosic biomasses have been used for biofuels, mainly bio-ethanol. The abundant avaiability of the raw material make the use of biomasses ideal. With the rise of carbon emission, biomasses can be used to substitue the need for carbon based fuel, as long as, the biomass is carbon neutral ^[3]. Lignostilbene is the second most abundant raw material.

Energy Transformation

When Phe 59 is substituted with His and Tyr 101 is substituted with Phe, the k (app/cat) decreases in activity by 15-10 folds. The Lys 134 substitution of Met inhibits the enzyme activity. Phenylazophenol inhibits the LsdA-catalyzed cleavage of lignostilbene with a competitive and uncompetitive inhibition.

Structural highlights

and

There are in each Chain. Lignostilbene is a quationary structure with two identical working together. The proteins are partially composed of (Blue) and the majority by indicated in red.