CAZypedia needs your help!
We have many unassigned pages in need of Authors and Responsible Curators. See a page that's out-of-date and just needs a touch-up? - You are also welcome to become a CAZypedian. Here's how.
Scientists at all career stages, including students, are welcome to contribute.
Learn more about CAZypedia's misson here and in this article.
Totally new to the CAZy classification? Read this first.

Difference between revisions of "Polysaccharide Lyase Family 32"

From CAZypedia
Jump to navigation Jump to search
m (Text replacement - "\^\^\^(.*)\^\^\^" to "$1")
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
 
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
 
<!-- RESPONSIBLE CURATORS: Please replace the {{UnderConstruction}} tag below with {{CuratorApproved}} when the page is ready for wider public consumption -->
{{UnderConstruction}}
+
{{CuratorApproved}}  
 
* [[Author]]: [[User:Marie-Line Garron|Marie-Line Garron]]
 
* [[Author]]: [[User:Marie-Line Garron|Marie-Line Garron]]
 
* [[Responsible Curator]]:  [[User:Marie-Line Garron|Marie-Line Garron]]
 
* [[Responsible Curator]]:  [[User:Marie-Line Garron|Marie-Line Garron]]
 
----
 
----
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 
<div style="float:right">
 
{| {{Prettytable}}
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL32'''
 
|-
 
|'''3D Structure'''   
 
|
 
|-
 
|'''Mechanism'''   
 
|
 
|-
 
|'''Charge neutraliser'''
 
|
 
|-
 
|'''Active site residues'''
 
|
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
|-
 
| colspan="2" |{{CAZyDBlink}}PL32.html
 
|}
 
</div>
 
<!-- This is the end of the table -->
 
  
  
 
== Substrate specificities ==
 
== Substrate specificities ==
Content is to be added here.
+
The PL32 family was created following the functional characterization of the ORF “HMPREF1071_02769” from ''Bacteroides salyersiae ''CL02T12C01 (EIY62149.1), which showed endo-mannuronan lyase activity ([https://www.enzyme-database.org/query.php?ec=4.2.2.3 EC 4.2.2.3]) <cite>Helbert2019</cite>. Shortly afterwards, the sequence was <u>'''reclassified'''</u> as  [http://www.cazy.org/PL0.html PL_nc]  on the basis of structural modelling revealing that the catalytic domain was restricted to the N-terminal domain <cite>Drula2022</cite>. The small number of sequences and the proximity to the PL14 and PL36 families do not allow the creation of a new PL family.
  
Authors may get an idea of what to put in each field from ''Curator Approved'' [[Polysaccharide Lyase Families]]. ''(TIP: Right click with your mouse and open this link in a new browser window...)''
+
== References ==
 +
<biblio>
 +
#Helbert2019 pmid=30850540
  
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
+
#Drula2022 pmid=34850161
  
== 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 ==
 
<biblio>
 
#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. [https://doi.org/10.1042/BIO03004026 Download PDF version].
 
 
</biblio>
 
</biblio>
  
 
[[Category:Polysaccharide Lyase Families|PL032]]
 
[[Category:Polysaccharide Lyase Families|PL032]]

Latest revision as of 08:31, 23 August 2024

Approve icon-50px.png

This page has been approved by the Responsible Curator as essentially complete. CAZypedia is a living document, so further improvement of this page is still possible. If you would like to suggest an addition or correction, please contact the page's Responsible Curator directly by e-mail.



Substrate specificities

The PL32 family was created following the functional characterization of the ORF “HMPREF1071_02769” from Bacteroides salyersiae CL02T12C01 (EIY62149.1), which showed endo-mannuronan lyase activity (EC 4.2.2.3) [1]. Shortly afterwards, the sequence was reclassified as PL_nc on the basis of structural modelling revealing that the catalytic domain was restricted to the N-terminal domain [2]. The small number of sequences and the proximity to the PL14 and PL36 families do not allow the creation of a new PL family.

References

  1. 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 | PubMed ID:30850540 [Helbert2019]
  2. Drula E, Garron ML, Dogan S, Lombard V, Henrissat B, and Terrapon N. (2022). The carbohydrate-active enzyme database: functions and literature. Nucleic Acids Res. 2022;50(D1):D571-D577. DOI:10.1093/nar/gkab1045 | PubMed ID:34850161 [Drula2022]

All Medline abstracts: PubMed