Sandbox Reserved 1568: Difference between revisions
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Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules. | Though lignin is the second most abundant fraction byproduct of lignocellulose, it is currently mostly just combusted for steam and electricity generation. It is rarely valorized into other products like a dispersant for cement and gypsum. One major difficulty in converting and valorizing lignin-based byproducts it their highly variable composition. Both the substrate in which they are located, and the means of extraction affect their end composition and properties. There is much research into finding strong methods of breakdown of lignostilbenoid molecules. | ||
== '''Structural highlights and structure-function relationships''' == | == '''Structural highlights and structure-function relationships''' == | ||
LsdA appears when crystallized as two LsdA protomers in one asymmetric unit as a dimer. The <scene name='82/823092/Secondary_and_tertiary_struct/1'>secondary and tertiary structure</scene> of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a seven-bladed ß-propeller, typical of the carotenoid cleavage oxygenases. | LsdA appears, when crystallized, as two LsdA protomers in one asymmetric unit as a dimer. The <scene name='82/823092/Secondary_and_tertiary_struct/1'>secondary and tertiary structure</scene> of the protomer consists of α-helices (purple) and ß-sheets (blue). The ß-sheets are arranged in a <scene name='82/823092/Seven-bladed_beta_propeller/1'>seven-bladed ß-propeller</scene>, typical of the carotenoid cleavage oxygenases. | ||
The <scene name='82/823092/Catalytic_triad/1'>catalytic triad</scene> of the binding site consists of Phe59, Tyr101, and Lys134 that contact the 4-hydroxyphenyl portion of the substrate. | |||
== '''Energy Transformation''' == | == '''Energy Transformation''' == | ||
