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Difference between revisions of "Polysaccharide Lyase Family 34"
Harry Brumer (talk | contribs) (Fixed CAZy link in table) |
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
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| − | | colspan="2" |{{CAZyDBlink}} | + | | colspan="2" |{{CAZyDBlink}}PL34.html |
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</div> | </div> | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | PL34 is a small family (28 sequences), mainly bacterial, with only one sequence belonging to the metazoan ''Knipowitschia caucasica'' | + | PL34 is a small family (28 sequences), mainly bacterial, with only one sequence belonging to the metazoan ''Knipowitschia caucasica''. The founding member of family 34, and the only one characterized, belongs to OPIT5_18480 of Opitutaceae bacterium TAV5 (AHF91913.1). This enzyme presents an activity against alginate (EC 4.2.2.-) <cite>Helbert2019</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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== References == | == References == | ||
<biblio> | <biblio> | ||
| − | |||
#Helbert2019 pmid=30850540 | #Helbert2019 pmid=30850540 | ||
</biblio> | </biblio> | ||
[[Category:Polysaccharide Lyase Families|PL034]] | [[Category:Polysaccharide Lyase Families|PL034]] | ||
Latest revision as of 15:46, 1 October 2024
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| Polysaccharide Lyase Family PL33 | |
| 3D Structure | |
| Mechanism | |
| Charge neutraliser | |
| Active site residues | |
| CAZy DB link | |
| https://www.cazy.org/PL34.html | |
Substrate specificities
PL34 is a small family (28 sequences), mainly bacterial, with only one sequence belonging to the metazoan Knipowitschia caucasica. The founding member of family 34, and the only one characterized, belongs to OPIT5_18480 of Opitutaceae bacterium TAV5 (AHF91913.1). This enzyme presents an activity against alginate (EC 4.2.2.-) [1].
Kinetics and Mechanism
Not determined
Catalytic Residues
Not determined
Three-dimensional structures
Unsolved
Family Firsts
- First description of catalytic activity
- Alginate lyase was the first activity discovered for the family PL34 [1].
- First First charge neutralizer identification
- To be determined
- First Brønstead acid and base residue identification
- To be determined
- First 3-D structure
- To be determined
References
- Helbert W, Poulet L, Drouillard S, Mathieu S, Loiodice M, Couturier M, Lombard V, Terrapon N, Turchetto J, Vincentelli R, and Henrissat B. (2019). Discovery of novel carbohydrate-active enzymes through the rational exploration of the protein sequences space. Proc Natl Acad Sci U S A. 2019;116(13):6063-6068. DOI:10.1073/pnas.1815791116 |