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Difference between revisions of "Polysaccharide Lyase Family 30"

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{| {{Prettytable}}  
 
{| {{Prettytable}}  
 
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|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL10'''
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|{{Hl2}} colspan="2" align="center" |'''Polysaccharide Lyase Family PL30'''
 
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|'''3D Structure'''     
 
|'''3D Structure'''     
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== Substrate specificities ==
 
== Substrate specificities ==
Content is to be added here.
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PL30 is a small family (38 sequences), exclusively bacterial belonging to the phylum ''Bacteroidetes''. The founding member of family 30, and the only one characterized, belongs to ''Bacteroides cellulosilyticus WH2 (BcellWH2_02524, ''WP_029426181.1). The activity was measured against hyaluronic acid by following the absorbance at 232nm. The increase in absorbance confirms that  ''BcellWH2_02524 ''is a hyaluronan lyase ([https://www.enzyme-database.org/query.php?ec=4.2.2.1 4.2.2.1]), probably using the by &beta;-elimination process like all PL families <cite>Helbert2019</cite>.  
 
 
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 ==
 
== Kinetics and Mechanism ==
Content is to be added here.
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Not Determined
  
 
== Catalytic Residues ==
 
== Catalytic Residues ==
Content is to be added here.
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Not Determined
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
Content is to be added here.
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Unsolved
  
 
== Family Firsts ==
 
== Family Firsts ==
;First stereochemistry determination: Content is to be added here.
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;First description of catalytic activity: Hyaluronan lyase was the first activity discovered for the family PL30 <cite>Helbert2019</cite>.
;First catalytic nucleophile identification: Content is to be added here.
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;First charge neutralizer identification: To be determined
;First general acid/base residue identification: Content is to be added here.
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;First Brønstead acid and base residue identification: To be determinated
;First 3-D structure: Content is to be added here.
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;First 3-D structure: To be determinated
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Cantarel2009 pmid=18838391
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#Helbert2019 pmid=30850540
#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:Glycoside Hydrolase Families|PL030]]
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[[Category:Polysaccharide Lyase Families|PL030]]

Latest revision as of 15:47, 1 October 2024

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Polysaccharide Lyase Family PL30
3D Structure
Mechanism
Charge neutraliser
Active site residues
CAZy DB link
https://www.cazy.org/PL30.html


Substrate specificities

PL30 is a small family (38 sequences), exclusively bacterial belonging to the phylum Bacteroidetes. The founding member of family 30, and the only one characterized, belongs to Bacteroides cellulosilyticus WH2 (BcellWH2_02524, WP_029426181.1). The activity was measured against hyaluronic acid by following the absorbance at 232nm. The increase in absorbance confirms that BcellWH2_02524 is a hyaluronan lyase (4.2.2.1), probably using the by β-elimination process like all PL families [1].

Kinetics and Mechanism

Not Determined

Catalytic Residues

Not Determined

Three-dimensional structures

Unsolved

Family Firsts

First description of catalytic activity
Hyaluronan lyase was the first activity discovered for the family PL30 [1].
First charge neutralizer identification
To be determined
First Brønstead acid and base residue identification
To be determinated
First 3-D structure
To be determinated

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]