Polysaccharide Lyase Family 2

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• Author: ^^^Wade Abbott^^^
• Responsible Curator: ^^^Wade Abbott^^^

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Polysaccharide Lyase Family PL2
Mechanism	β-elimination
Metal Cofactor	Manganese
Active site residues	known
CAZy DB link
https://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.

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

YpseuPL2/PelY from Yersinia pseudotuberculosis macerated cucumber [3].

First catalytic base identification

PL2A (YE4069)Arg218 from Yersinia enterocolitica [2].

First catalytic divalent cation identification

DdPL2/PelW(Dda3937_03361) from Dickiya Dadantii 3937 (Previously Erwinia chrysanthemi 3937)

First 3-D structure

PL2A (YE4069) from Yersinia enterocolitica [2].

References

1. 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

2. 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 |
3. Manulis S, Kobayashi DY, and Keen NT. (1988). Molecular cloning and sequencing of a pectate lyase gene from Yersinia pseudotuberculosis. J Bacteriol. 1988;170(4):1825-30. DOI:10.1128/jb.170.4.1825-1830.1988 |
4. Shevchik VE, Condemine G, Robert-Baudouy J, and Hugouvieux-Cotte-Pattat N. (1999). The exopolygalacturonate lyase PelW and the oligogalacturonate lyase Ogl, two cytoplasmic enzymes of pectin catabolism in Erwinia chrysanthemi 3937. J Bacteriol. 1999;181(13):3912-9. DOI:10.1128/JB.181.13.3912-3919.1999 |