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Difference between revisions of "Glycoside Hydrolase Family 189"
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== Substrate specificities == | == Substrate specificities == | ||
| − | + | The cyclization domain alone of cyclic β-1,2-glucan synthase from Thermoanaerobacter italicus (TiCGSCy) was identified, characterized and structurally analyzed as reported in 2024 [1]. This enzyme established the novel glycoside hydrolase family (GH) 189. This enzyme specifically catalyzes transglycosylation reactions on linear β-1,2-glucans (LβGs) and β-1,2-glucooligosaccharides (Sopns, where 'n' represents the degree of polymerization (DP)) with DP 6 or more [1]. In the deglycosylation step, intermolecular transglycosylation results in release of disproportionated linear products, while intramolecular transglycosylation results in cyclization of the substrates to release cyclic β-1,2-glucans (CβGs) [1]. | |
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== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
Revision as of 19:09, 1 February 2024
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.
- Authors: Tomoko Masaike, Masahiro Nakajima, and Nobukiyo Tanaka
- Responsible Curator: Masahiro Nakajima
| Glycoside Hydrolase Family GH189 | |
| Clan | GH-x |
| Mechanism | retaining |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/GH189.html | |
Substrate specificities
The cyclization domain alone of cyclic β-1,2-glucan synthase from Thermoanaerobacter italicus (TiCGSCy) was identified, characterized and structurally analyzed as reported in 2024 [1]. This enzyme established the novel glycoside hydrolase family (GH) 189. This enzyme specifically catalyzes transglycosylation reactions on linear β-1,2-glucans (LβGs) and β-1,2-glucooligosaccharides (Sopns, where 'n' represents the degree of polymerization (DP)) with DP 6 or more [1]. In the deglycosylation step, intermolecular transglycosylation results in release of disproportionated linear products, while intramolecular transglycosylation results in cyclization of the substrates to release cyclic β-1,2-glucans (CβGs) [1].
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 stereochemistry determination
- Content is to be added here.
- First catalytic nucleophile identification
- Content is to be added here.
- First general acid/base residue identification
- Content is to be added here.
- First 3-D structure
- Content is to be added here.
References
- 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 |
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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. DOI:10.1042/BIO03004026.