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Difference between revisions of "Polysaccharide Lyase Family 38"

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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...)''
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In the meantime, please see these references for an essential introduction to the CAZy classification system: <cite>DaviesSinnott2008 Cantarel2009</cite>.
  
 
== Substrate specificities ==
 
== Substrate specificities ==
 
Content is to be added here.
 
Content is to be added here.
 
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 ==
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== Family Firsts ==
 
== Family Firsts ==
;First description of catalytic activity: (1,4)-β-D-glucuronan activity by ''Brevundimonas sp. SH203'' cellouronate lyase (CUL-I) <cite> kikuchi2019 </cite>.
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;First description of catalytic activity:  
;First catalytic nucleophile identification: Content is to be added here.
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*(1,4)-β-D-glucuronan activity by ''Brevundimonas sp. SH203'' cellouronate lyase (CUL-I) <cite> kikuchi2019 </cite>.
;First general acid/base residue identification: Content is to be added here.
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*Sodium-alginate, poly-mannuronate and poly-guluronate activity by ''Agarivorans sp. B2Z047'' alginate lyase (Aly38A) <cite> Sun2022 </cite>.
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;First catalytic base/acid: Content is to be added here.
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;First charge neutralizer: Content is to be added here.
 
;First 3-D structure: ''Bacteroides ovatus ATCC 8483'' PL38 (PDB [https://www.rcsb.org/structure/3NFV 3NFV] and [https://www.rcsb.org/structure/3NNB 3NNB]), published by the Joint Center for Structural Genomics ([http://www.jcsg.org JCSG]) [No associated publication].
 
;First 3-D structure: ''Bacteroides ovatus ATCC 8483'' PL38 (PDB [https://www.rcsb.org/structure/3NFV 3NFV] and [https://www.rcsb.org/structure/3NNB 3NNB]), published by the Joint Center for Structural Genomics ([http://www.jcsg.org JCSG]) [No associated publication].
  

Latest revision as of 02:42, 4 June 2024

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Polysaccharide Lyase Family 38
3D structure

( α / α )7 barrel

Mechanism

β-elimination

Charge neutralizer
Active site residues unknown
CAZy DB link
https://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