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Difference between revisions of "Polysaccharide Lyase Family 32"

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* [[Author]]: ^^^Marie-Line Garron^^^
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* [[Responsible Curator]]:  ^^^Marie-Line Garron^^^
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* [[Author]]: [[User:Marie-Line Garron|Marie-Line Garron]]
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* [[Responsible Curator]]:  [[User:Marie-Line Garron|Marie-Line Garron]]
 
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=== PL32 is a deleted family ===
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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 ([{{EClink}}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. 
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== References ==
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<biblio>
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#Helbert2019 pmid=30850540
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#Drula2022 pmid=34850161
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</biblio>
 
<!-- The data in the table below should be updated by the Author/Curator according to current information on the family -->
 
<!-- 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}}  
 
{| {{Prettytable}}  
 
|-
 
|-
|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL32'''
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB links'''
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|'''3D Structure'''   
 
|
 
|-
 
|'''Mechanism'''   
 
|
 
|-
 
|'''Charge neutraliser'''
 
|
 
|-
 
|'''Active site residues'''
 
|
 
|-
 
|{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
 
 
|-
 
|-
 
| colspan="2" |{{CAZyDBlink}}PL32.html
 
| colspan="2" |{{CAZyDBlink}}PL32.html
 
|}
 
|}
</div>
 
 
<!-- This is the end of the table -->
 
<!-- This is the end of the table -->
 
 
== Substrate specificities ==
 
Content is to be added here.
 
 
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...)''
 
 
In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
 
 
== 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>
 
  
 
[[Category:Polysaccharide Lyase Families|PL032]]
 
[[Category:Polysaccharide Lyase Families|PL032]]

Latest revision as of 15:42, 1 October 2024

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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.

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This family has been deleted from the CAZy classification. A specific explanation may be found below.


PL32 is a deleted family

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

CAZy DB links
https://www.cazy.org/PL32.html