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Difference between revisions of "Polysaccharide Lyase Family 30"

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* [[Author]]: [[User:Marie-Line Garron|Marie-Line Garron]]
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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'' ([http://www.cazy.org/PL30.html PL30]) <cite>Drula2022</cite>. 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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#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].
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#Drula2022 pmid=34850161
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 +
#Helbert2019 pmid=30850540
 
</biblio>
 
</biblio>
  
 
[[Category:Polysaccharide Lyase Families|PL030]]
 
[[Category:Polysaccharide Lyase Families|PL030]]

Latest revision as of 08:31, 23 August 2024

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


Substrate specificities

PL30 is a small family (38 sequences), exclusively bacterial belonging to the phylum Bacteroidetes (PL30) [1]. 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 [2].

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 [2].
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. 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]
  2. 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]

All Medline abstracts: PubMed