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Difference between revisions of "Polysaccharide Lyase Family 2"
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|'''Mechanism''' | |'''Mechanism''' | ||
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|'''Metal Cofactor''' | |'''Metal Cofactor''' | ||
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== Three-dimensional structures == | == Three-dimensional structures == | ||
| − | The structure of the endolytic PL2A from ''Yersinia enterocolitica'' (YePL2A) is the only only PL2 structure to be reported <cite>Abbott2007</cite>. Three different models for YePL2A have been deposited, including a native-form (2V8I, 1.50 Å), and a complex with trigalacturonate (2V8K, 2.1 Å) and a transitional metal (2V8J, 2.01 Å). Family 2 PLs adopt a rare alpha/alpha-7 barrel fold, with an active site cleft extending along the surface of the enzyme between two catalytic arms. The active site centre, consisting of the metal coordination pocket and catalytic arginines, is positioned at one end of the cleft. Substrate binding induces a conformational change and the arms close about the substrate. | + | The structure of the endolytic PL2A from ''Yersinia enterocolitica'' (YePL2A) is the only only PL2 structure to be reported <cite>Abbott2007</cite>. Three different models for YePL2A have been deposited, including a native-form (2V8I, 1.50 Å), and a complex with trigalacturonate (2V8K, 2.1 Å) and a transitional metal (2V8J, 2.01 Å). Family 2 PLs adopt a rare α/α-7 barrel fold, with an active site cleft extending along the surface of the enzyme between two catalytic arms. The active site centre, consisting of the metal coordination pocket and catalytic arginines, is positioned at one end of the cleft. Substrate binding induces a conformational change and the arms close about the substrate. |
== Family Firsts == | == Family Firsts == | ||
Revision as of 14:17, 20 September 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: ^^^Wade Abbott^^^
- Responsible Curator: ^^^Wade Abbott^^^
| Polysaccharide Lyase Family PL2 | |
| Mechanism | β-elimination |
| Metal Cofactor | Manganese |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/PL2.html | |
Substrate specificities
Content is to be added here.
Authors may get an idea of what to put in each field from Curator Approved Glycoside Hydrolase Families. (TIP: Right click with your mouse and open this link in a new browser window...)
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.
Subfamilies
Three-dimensional structures
The structure of the endolytic PL2A from Yersinia enterocolitica (YePL2A) is the only only PL2 structure to be reported [2]. Three different models for YePL2A have been deposited, including a native-form (2V8I, 1.50 Å), and a complex with trigalacturonate (2V8K, 2.1 Å) and a transitional metal (2V8J, 2.01 Å). Family 2 PLs adopt a rare α/α-7 barrel fold, with an active site cleft extending along the surface of the enzyme between two catalytic arms. The active site centre, consisting of the metal coordination pocket and catalytic arginines, is positioned at one end of the cleft. Substrate binding induces a conformational change and the arms close about the substrate.
Family Firsts
- First catalytic activity
- Content is to be added here.
- First catalytic base identification
- Content is to be added here.
- First catalytic divalent cation identification
- Content is to be added here.
- First 3-D structure
- PL2A from Yersinia enterocolitica [2].
References
-
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
- Abbott DW and Boraston AB. (2007). A family 2 pectate lyase displays a rare fold and transition metal-assisted beta-elimination. J Biol Chem. 2007;282(48):35328-36. DOI:10.1074/jbc.M705511200 |