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Polysaccharide Lyase Family 38

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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 38
3D structure

( α / α )7 barrel

Mechanism

β-elimination

Charge neutralizer
Active site residues unknown
CAZy DB link
http://www.cazy.org/PL38.html

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].

Substrate specificities

Content is to be added here.

Kinetics and Mechanism

Content is to be added here.

Catalytic Residues

Content is to be added here.

Three-dimensional structures

Content is to be added here.

Family Firsts

First description of catalytic activity
  • (1,4)-β-D-glucuronan activity by Brevundimonas sp. SH203 cellouronate lyase (CUL-I) [3].
  • Sodium-alginate, poly-mannuronate and poly-guluronate activity by Agarivorans sp. B2Z047 alginate lyase (Aly38A) [4].
First catalytic base/acid
Content is to be added here.
First charge neutralizer
Content is to be added here.
First 3-D structure
Bacteroides ovatus ATCC 8483 PL38 (PDB 3NFV and 3NNB), published by the Joint Center for Structural Genomics (JCSG) [No associated publication].

References

  1. 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. [1].

    [DaviesSinnott2008]
  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 | PubMed ID:18838391 [Cantarel2009]
  3. Kikuchi M, Konno N, Suzuki T, Fujii Y, Kodama Y, Isogai A, and Habu N. (2020). A bacterial endo-β-1,4-glucuronan lyase, CUL-I from Brevundimonas sp. SH203, belonging to a novel polysaccharide lyase family. Protein Expr Purif. 2020;166:105502. DOI:10.1016/j.pep.2019.105502 | PubMed ID:31546007 [kikuchi2019]
  4. Sun XK, Gong Y, Shang DD, Liu BT, Du ZJ, and Chen GJ. (2022). Degradation of Alginate by a Newly Isolated Marine Bacterium Agarivorans sp. B2Z047. Mar Drugs. 2022;20(4). DOI:10.3390/md20040254 | PubMed ID:35447927 [Sun2022]
  5. Pilgaard B, Vuillemin M, Munk L, Holck J, Meier S, Wilkens C, and Meyer AS. (2022). Discovery of a Novel Glucuronan Lyase System in Trichoderma parareesei. Appl Environ Microbiol. 2022;88(1):e0181921. DOI:10.1128/AEM.01819-21 | PubMed ID:34705548 [Pilgaard2022]
  6. Rønne ME, Tandrup T, Madsen M, Hunt CJ, Myers PN, Moll JM, Holck J, Brix S, Strube ML, Aachmann FL, Wilkens C, and Svensson B. (2023). Three alginate lyases provide a new gut Bacteroides ovatus isolate with the ability to grow on alginate. Appl Environ Microbiol. 2023;89(10):e0118523. DOI:10.1128/aem.01185-23 | PubMed ID:37791757 [Ronne2023]

All Medline abstracts: PubMed