Chondroitin lyases have been known as pathogenic bacterial enzymes that degrade chondroitin. Recently, baculovirus envelope protein ODV-E66 was identified as the first reported viral chondroitin lyase. ODV-E66 has low sequence identity with bacterial lyases at <12%, and unique characteristics reflecting the life cycle of baculovirus. To understand ODV-E66's structural basis, the crystal structure was determined and it was found that the structural fold resembled that of polysaccharide lyase 8 proteins and that the catalytic residues were also conserved. This structure enabled discussion of the unique substrate specificity and the stability of ODV-E66 as well as the host specificity of baculovirus.
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Article Synopsis
- - Dermatan sulfate and chondroitin sulfate are dietary supplements that can help prevent blood clots, with low-molecular-weight dermatan sulfate (LMWDS) being especially effective due to its high absorption rate.
- - The study explored improving the efficiency of chondroitin B lyases, which are enzymes used to create LMWDS, by engineering their substrate-binding domain through a design strategy that involved modifying specific amino acids.
- - Four mutations showed significant increases in enzyme activity, and the combination of two mutations (H134Y/R159K) resulted in a dramatic 3.21-fold enhancement, potentially making these enzymes more useful in pharmaceuticals and food products.
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