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Difference between revisions of "Polysaccharide Lyase Family 17"
Harry Brumer (talk | contribs) (Created page with " <!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption --> {{UnderConstruc...") |
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|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family 17''' | |{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family 17''' | ||
|- | |- | ||
| − | |''' | + | |'''3D structure''' |
| − | | | + | |(α/α)6 barrel + anti-parallel β-sheet |
|- | |- | ||
|'''Mechanism''' | |'''Mechanism''' | ||
| − | | | + | |β-eliminationg |
| + | |-|- | ||
| + | |'''Charge neutralizer''' | ||
| + | |Asparagine and histidine | ||
|- | |- | ||
|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |known |
|- | |- | ||
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
| Line 30: | Line 33: | ||
== 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 | |
| − | |||
| − | |||
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. | In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>. | ||
| Line 53: | Line 54: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| + | |||
| + | #Lombard2010 pmid=20925655 | ||
| + | #Jagtap2014 pmid=24795372 | ||
| + | #Park2014 pmid=24478312 | ||
| + | #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 | ||
| + | #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 | ||
#Cantarel2009 pmid=18838391 | #Cantarel2009 pmid=18838391 | ||
#DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | #DaviesSinnott2008 Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. ''The Biochemist'', vol. 30, no. 4., pp. 26-32. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version]. | ||
Revision as of 01:21, 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 In the meantime, please see these references for an essential introduction to the CAZy classification system: [2, 3].
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
-
Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.
- Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |
- 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 |
- 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 |
-
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 |
-
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