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Polysaccharide Lyase Family 30

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This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.


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 (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