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Difference between revisions of "Polysaccharide Lyase Family 8"
| Line 13: | Line 13: | ||
|- | |- | ||
|'''''3D Structure''''' | |'''''3D Structure''''' | ||
| − | |(alpha/alpha)<sub>6</sub> barrel + anti-parallel beta-sheet | + | |(α/α)<sub>6</sub> barrel + anti-parallel β-sheet |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | |beta-elimination | + | |β-elimination |
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| Line 32: | Line 32: | ||
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). | 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 == | == Substrate specificities == | ||
| − | |||
| − | + | PL8 activity has been demonstrated on a variety of uronic acid-containing polysaccharides including <u>'''hyaluronan'''</u> [4)-β-D-Glucuronate-1,3-β -D-N-Acetyl-Glucosamine(1]<sub>n</sub>, <u>'''chondroitin AC'''</u> [4)-β-D-Glucuronate-1,3-β-D-N-Acetyl-GalactosamineΔ4,6S(1]<sub>n</sub>, <u>'''xanthan'''</u> [4)-β-D-Glucuronate-1,4-β-D-Glucuronate (1]<sub>n</sub>, and <u>'''chondroitin ABC'''</u> [chondroitin AC and chondroitin B (aka. dermatan sulfate: 4)-β-L-Iduronate2S-1,3-β-D-N-Acetyl-Galactosamine4S(1]<sub>n</sub>. | |
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. | In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. | ||
Revision as of 07:14, 6 November 2013
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- 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.
In the meantime, please see these references for an essential introduction to the CAZy classification system: [1, 2].
Kinetics and Mechanism
Content is to be added here.
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
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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
- 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 |