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Difference between revisions of "Carbohydrate Binding Module Family 92"

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== References ==
 
== References ==
 
<biblio>
 
<biblio>
#Mei2022 pmid=35830544
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#Cantarel2009 pmid=18838391
#Shen2018 pmid=29355636
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#DaviesSinnott2008 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. [http://www.biochemist.org/bio/03004/0026/030040026.pdf Download PDF version].
 
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#Boraston2004 pmid=15214846
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#Hashimoto2006 pmid=17131061
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#Shoseyov2006 pmid=16760304
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#Guillen2010 pmid=19908036
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#Armenta2017 pmid=28547780
 
</biblio>
 
</biblio>
  
  
 
[[Category:Carbohydrate Binding Module Families|CBM092]]
 
[[Category:Carbohydrate Binding Module Families|CBM092]]

Revision as of 00:59, 27 January 2023

Cite error: Invalid <ref> tag; refs with no name must have content

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CAZy DB link
https://www.cazy.org/CBM92.html

Ligand specificities

The first and only hereinto characterized member in the CBM92 family is Cgk16A-CBM92 [1]. The CBM could specifically bind to carrageenan and showed no significant difference in the affinity to κ- and ι-carrageenan.

Structural Features

No three-dimensional structure has been solved in this CBM family at present.

Functionalities

A carrageenan-specific fluorescent probe was successfully constructed by fusing Cgk16A-CBM92 with a green fluorescent protein. The in situ visualization of carrageenan in red alga Kappaphycus alvarezii was realized by utilizing the fluorescent probe [1].

Family Firsts

First Identified

The first member Cgk16A-CBM92 is a component of a κ-carrageenase Cgk16A [2], which was discovered from a marine bacterium Wenyingzhuangia aestuarii OF219.

References

  1. 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]
  2. 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. Download PDF version.

    [DaviesSinnott2008]
  3. Boraston AB, Bolam DN, Gilbert HJ, and Davies GJ. (2004). Carbohydrate-binding modules: fine-tuning polysaccharide recognition. Biochem J. 2004;382(Pt 3):769-81. DOI:10.1042/BJ20040892 | PubMed ID:15214846 [Boraston2004]
  4. Hashimoto H (2006). Recent structural studies of carbohydrate-binding modules. Cell Mol Life Sci. 2006;63(24):2954-67. DOI:10.1007/s00018-006-6195-3 | PubMed ID:17131061 [Hashimoto2006]
  5. Shoseyov O, Shani Z, and Levy I. (2006). Carbohydrate binding modules: biochemical properties and novel applications. Microbiol Mol Biol Rev. 2006;70(2):283-95. DOI:10.1128/MMBR.00028-05 | PubMed ID:16760304 [Shoseyov2006]
  6. Guillén D, Sánchez S, and Rodríguez-Sanoja R. (2010). Carbohydrate-binding domains: multiplicity of biological roles. Appl Microbiol Biotechnol. 2010;85(5):1241-9. DOI:10.1007/s00253-009-2331-y | PubMed ID:19908036 [Guillen2010]
  7. Armenta S, Moreno-Mendieta S, Sánchez-Cuapio Z, Sánchez S, and Rodríguez-Sanoja R. (2017). Advances in molecular engineering of carbohydrate-binding modules. Proteins. 2017;85(9):1602-1617. DOI:10.1002/prot.25327 | PubMed ID:28547780 [Armenta2017]

All Medline abstracts: PubMed