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Polysaccharide Lyase Family 8
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- Author: ^^^Michael Suits^^^
- Responsible Curator: ^^^Michael Suits^^^
Polysaccharide Lyase Family PL8 | |
3D Structure | (α/α)6 barrel + anti-parallel β-sheet |
Mechanism | β-elimination |
Active site residues | known/not known |
CAZy DB link | |
https://www.cazy.org/PL8.html |
Known Activities
hyaluronate lyase (EC 4.2.2.1); chondroitin AC lyase (EC 4.2.2.5); xanthan lyase (EC 4.2.2.12); chondroitin ABC lyase (EC 4.2.2.20).
Substrate specificities
PL8 activity has been demonstrated on a variety of uronic acid-containing polysaccharides including hyaluronan [4)-β-D-Glucuronate-1,3-β -D-N-Acetyl-Glucosamine(1]n, chondroitin AC [4)-β-D-Glucuronate-1,3-β-D-N-Acetyl-GalactosamineΔ4,6S(1]n, xanthan [4)-β-D-Glucuronate-1,4-β-D-Glucuronate (1]n, and chondroitin ABC [chondroitin AC and chondroitin B (aka. dermatan sulfate: 4)-β-L-Iduronate2S-1,3-β-D-N-Acetyl-Galactosamine4S(1]n.
Kinetics and Mechanism
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Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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References
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
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Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382