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Difference between revisions of "Carbohydrate Binding Module Family 92"
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The first member Cgk16A-CBM92 is a component of a κ-carrageenase Cgk16A [2], which was discovered from a marine bacterium ''Wenyingzhuangia aestuarii'' OF219. | 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 == | ||
| + | <biblio> | ||
| + | #Oka2022 pmid=36106687 | ||
| + | #Nagae2022 pmid=35854001 | ||
| + | #Osada2022 pmid=35988645 | ||
| + | |||
| + | |||
| + | </biblio> | ||
| + | <!-- Do not delete this Category tag --> | ||
| + | [[Category:Carbohydrate Binding Module Families|CBM092]] | ||
Revision as of 01:01, 27 January 2023
Cite error: Invalid <ref> tag; refs with no name must have content
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.
| 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
- Oka N, Mori S, Ikegaya M, Park EY, and Miyazaki T. (2022). Crystal structure and sugar-binding ability of the C-terminal domain of N-acetylglucosaminyltransferase IV establish a new carbohydrate-binding module family. Glycobiology. 2022;32(12):1153-1163. DOI:10.1093/glycob/cwac058 |
- Nagae M, Hirata T, Tateno H, Mishra SK, Manabe N, Osada N, Tokoro Y, Yamaguchi Y, Doerksen RJ, Shimizu T, and Kizuka Y. (2022). Discovery of a lectin domain that regulates enzyme activity in mouse N-acetylglucosaminyltransferase-IVa (MGAT4A). Commun Biol. 2022;5(1):695. DOI:10.1038/s42003-022-03661-w |
- Osada N, Nagae M, Nakano M, Hirata T, and Kizuka Y. (2022). Examination of differential glycoprotein preferences of N-acetylglucosaminyltransferase-IV isozymes a and b. J Biol Chem. 2022;298(9):102400. DOI:10.1016/j.jbc.2022.102400 |