Polysaccharide Lyase Family 44

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• Author: Jinhang Zhou
• Responsible Curator: Yaoguang Chang

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Polysaccharide Lyase Family PL44
3D Structure
Mechanism
Charge neutraliser
Active site residues
CAZy DB link
https://www.cazy.org/PL44.html

Substrate specificities

Members of polysaccharide lyase family 44 have been shown to exhibit alginate lyase activity. The first member of this family is Aly44A, which originates from the bacterium Bacillus sp. FJAT-50079. (Genbank number WP_213137828.1). A total of 126 homologous sequences of Aly44A were identified by utilizing the BLASTp (with sequence coverage > 70% and identity > 40%) and CD-Hit tools. Meanwhile, four homologs of Aly44A exhibited the ability to degrade alginate (Zhou et al., 2024).

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: [1, 2].

Kinetics and Mechanism

The kinetic analysis showed that Aly44A exhibited higher conversion efficiency and a stronger affinity for polyM compared to polyG, indicating Aly44A was polyM-preferred. In contrast to bifunctional alginate lyases, which exhibited no preference for polyG or polyM, Aly44A showed superior potential in the preparation of alginate oligosaccharides consisting of M-blocks. It showed that Aly44A had a higher affinity and catalytic efficiency towards the polyM region of the longer-chain alginate (Zhou et al., 2024).

Action Pattern

Based on the analysis of the action pattern, it showed that Aly44A was polyM-preferred. Aly44A was verified to exhibit a random endo-acting lyase activity to alginate. The final products of degradation were alginate oligosaccharides with DP 2-8, the main products of degradation were AOS with DP 2-4 as detected by UPSEC-MS (Zhou et al., 2024).

Catalytic Residues

No catalytic residues have been identified in this polysaccharide lyase family at present.

Three-dimensional structures

The structure of Aly44A was predicted to be a parallel β-helix by AlphaFold2 (Zhou et al., 2024).

Family Firsts

First description of catalytic activity

The alginate lyase Aly44A was the first member of the family PL44 to be identified and characterized.

First stereochemistry determination

Not yet identified.

First catalytic nucleophile identification

Not yet identified.

First general acid/base residue identification

Not yet identified.

First 3-D structure

Not yet identified.

References

2. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |

3. , J., Li, J., Chen, G., Zheng, L., Mei, X., Xue, C., & Chang, Y. (2024). Discovery and characterization of a novel poly-mannuronate preferred alginate lyase: The first member of a new polysaccharide lyase family. Carbohydrate Polymers, 343, 122474.Download PDF version.