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Difference between revisions of "Polysaccharide Lyase Family 17"
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== Substrate specificities == | == Substrate specificities == | ||
' | ' | ||
| − | PL17 currently contains 2 subfamilies <cite>lombard2010</cite> as well as several proteins currently not assigned to any subfamily. Subfamily 2 has been shown to be exolytic alginate lyases | + | PL17 currently contains 2 subfamilies <cite>lombard2010</cite> as well as several proteins currently not assigned to any subfamily. Subfamily 2 has been shown to be exolytic alginate lyases <cite>Jagtap2014,Park2014,Shin2015,Wang2015</cite> with specificity for all tree block structure observed <cite>Mathieu2018</cite>. |
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== References == | == References == | ||
<biblio> | <biblio> | ||
| − | |||
#Lombard2010 pmid=20925655 | #Lombard2010 pmid=20925655 | ||
#Jagtap2014 pmid=24795372 | #Jagtap2014 pmid=24795372 | ||
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#Shin2015 Shin, J. W., Lee, O. K., Park, H. H., Kim, H. S., and Lee, E. Y. (2015) Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification. Korean J. Chem. Eng. 32, 917–924 | #Shin2015 Shin, J. W., Lee, O. K., Park, H. H., Kim, H. S., and Lee, E. Y. (2015) Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification. Korean J. Chem. Eng. 32, 917–924 | ||
#Wang2015 pmid=25335746 | #Wang2015 pmid=25335746 | ||
| + | #Mathieu2018 pmid=29795267 | ||
#Haug1967 Haug, A., Larsen, B., and Smidsrod, O. (1967) Studies on sequence of uronic acid residues in alginic acid. Acta Chem. Scand. 21, 691–704 | #Haug1967 Haug, A., Larsen, B., and Smidsrod, O. (1967) Studies on sequence of uronic acid residues in alginic acid. Acta Chem. Scand. 21, 691–704 | ||
#Haug1966 Haug, A., Larsen, B., and Smidsrod, O. (1966) A study of constitution of alginic acid by partial acid hydrolysis. Acta Chem. Scand. 20, 183–190 | #Haug1966 Haug, A., Larsen, B., and Smidsrod, O. (1966) A study of constitution of alginic acid by partial acid hydrolysis. Acta Chem. Scand. 20, 183–190 | ||
| − | |||
</biblio> | </biblio> | ||
[[Category:Polysaccharide Lyase Families|PL017]] | [[Category:Polysaccharide Lyase Families|PL017]] | ||
Revision as of 01:26, 4 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.
- Author: ^^^Emil Stender^^^
- Responsible Curator: ^^^Birte Svensson^^^
| Polysaccharide Lyase Family 17 | |
| 3D structure | (α/α)6 barrel + anti-parallel β-sheet |
| Mechanism | β-eliminationg |
| Charge neutralizer | Asparagine and histidine |
| Active site residues | known |
| CAZy DB link | |
| https://www.cazy.org/PL17.html | |
Substrate specificities
' PL17 currently contains 2 subfamilies [1] as well as several proteins currently not assigned to any subfamily. Subfamily 2 has been shown to be exolytic alginate lyases [2, 3, 4, 5] with specificity for all tree block structure observed [6].
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
- Jagtap SS, Hehemann JH, Polz MF, Lee JK, and Zhao H. (2014). Comparative biochemical characterization of three exolytic oligoalginate lyases from Vibrio splendidus reveals complementary substrate scope, temperature, and pH adaptations. Appl Environ Microbiol. 2014;80(14):4207-14. DOI:10.1128/AEM.01285-14 |
- Park D, Jagtap S, and Nair SK. (2014). Structure of a PL17 family alginate lyase demonstrates functional similarities among exotype depolymerases. J Biol Chem. 2014;289(12):8645-55. DOI:10.1074/jbc.M113.531111 |
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Shin, J. W., Lee, O. K., Park, H. H., Kim, H. S., and Lee, E. Y. (2015) Molecular characterization of a novel oligoalginate lyase consisting of AlgL- and heparinase II/III-like domains from Stenotrophomonas maltophilia KJ-2 and its application to alginate saccharification. Korean J. Chem. Eng. 32, 917–924
- Wang L, Li S, Yu W, and Gong Q. (2015). Cloning, overexpression and characterization of a new oligoalginate lyase from a marine bacterium, Shewanella sp. Biotechnol Lett. 2015;37(3):665-71. DOI:10.1007/s10529-014-1706-z |
- Mathieu S, Touvrey-Loiodice M, Poulet L, Drouillard S, Vincentelli R, Henrissat B, Skjåk-Bræk G, and Helbert W. (2018). Ancient acquisition of "alginate utilization loci" by human gut microbiota. Sci Rep. 2018;8(1):8075. DOI:10.1038/s41598-018-26104-1 |
- 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 |
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Haug, A., Larsen, B., and Smidsrod, O. (1967) Studies on sequence of uronic acid residues in alginic acid. Acta Chem. Scand. 21, 691–704
-
Haug, A., Larsen, B., and Smidsrod, O. (1966) A study of constitution of alginic acid by partial acid hydrolysis. Acta Chem. Scand. 20, 183–190