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Polysaccharide Lyase Family 7

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Polysaccharide Lyase Family PL7
3D Structure β jelly roll
Mechanism β-elimination
Active site residues known
CAZy DB link
http://www.cazy.org/PL7.html

Substrate specificities

The polysaccharide lyase family 7 (PL7) contains 5 subfamilies [1]. All characterized PL7 enzymes were alginate lyases specific for the anionic, gel forming polysaccharide alginate which is from brown seaweed such as kelps or from certain types of bacteria. Alginate consists of beta-D-mannuronate and alpha-L-guluronate, which occur in homogenous or heterogenous blocks. Hence, PL7 can be mannuronate, guluronate or mixed link lyases. PL7 enzymes are often found in marine bacteria such as the seaweed associated Flavobacterium Zobellia galactanivorans [2] or in coastal, planktonic gammaproteobacteria such as Vibrio spp. PL7 alginate lyases also occur in terrestrial bacteria.

poly-(MG)-lyase / MG-specific alginate lyase (EC 4.2.2.-)

β-D-mannuronate lyase / M-specific alginate lyase (EC 4.2.2.3)

α-L-guluronate lyase / G-specific alginate lyase (EC 4.2.2.11)

endo-β-1,4-glucuronan lyase (EC 4.2.2.14)

Mechanism and catalytic Residues

β-elimination

Three-dimensional structures

Evolution of Aly PULs

[3]

Family Firsts

References

  1. Lombard V, Bernard T, Rancurel C, Brumer H, Coutinho PM, and Henrissat B. (2010). A hierarchical classification of polysaccharide lyases for glycogenomics. Biochem J. 2010;432(3):437-44. DOI:10.1042/BJ20101185 | PubMed ID:20925655 [Lombard2010]
  2. Thomas F, Lundqvist LC, Jam M, Jeudy A, Barbeyron T, Sandström C, Michel G, and Czjzek M. (2013). Comparative characterization of two marine alginate lyases from Zobellia galactanivorans reveals distinct modes of action and exquisite adaptation to their natural substrate. J Biol Chem. 2013;288(32):23021-37. DOI:10.1074/jbc.M113.467217 | PubMed ID:23782694 [Thomas2013]
  3. Hehemann JH, Correc G, Barbeyron T, Helbert W, Czjzek M, and Michel G. (2010). Transfer of carbohydrate-active enzymes from marine bacteria to Japanese gut microbiota. Nature. 2010;464(7290):908-12. DOI:10.1038/nature08937 | PubMed ID:20376150 [Hehemann2010]

All Medline abstracts: PubMed