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Difference between revisions of "Polysaccharide Lyase Family 7"
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The polysaccharide lyase family 7 (PL7) contains 5 subfamilies <cite>Lombard2010</cite>. 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 <cite>Thomas2013</cite> or in coastal, planktonic gammaproteobacteria such as Vibrio spp. PL7 alginate lyases also occur in terrestrial bacteria. | The polysaccharide lyase family 7 (PL7) contains 5 subfamilies <cite>Lombard2010</cite>. 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 <cite>Thomas2013</cite> 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 == | == Three-dimensional structures == | ||
Revision as of 05:18, 31 July 2019
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.
- Authors: ^^^Nadine Gerlach^^^ and ^^^Jan-Hendrik Hehemann^^^
- Responsible Curator: ^^^Jan-Hendrik Hehemann^^^
| Polysaccharide Lyase Family PL7 | |
| 3D Structure | β jelly roll |
| Mechanism | β-elimination |
| Active site residues | known |
| CAZy DB link | |
| https://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
Family Firsts
References
- 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 |
- 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 |