Polysaccharide Lyase Family 44

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.

• Author: Jinhang Zhou
• Responsible Curator: Yaoguang Chang

---

Polysaccharide Lyase Family PL44
3D Structure	parallel β-helix (AlphaFold)
Mechanism	poly-mannuronate preferred
Charge neutraliser	not known
Active site residues	not known
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 [1].

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 [1].

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 [1].

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 [1].

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

1. Zhou J, Li J, Chen G, Zheng L, Mei X, Xue C, and Chang Y. (2024). Discovery and characterization of a novel poly-mannuronate preferred alginate lyase: The first member of a new polysaccharide lyase family. Carbohydr Polym. 2024;343:122474. DOI:10.1016/j.carbpol.2024.122474 |