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Difference between revisions of "Glycoside Hydrolase Family 81"
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== Substrate specificities == | == Substrate specificities == | ||
GH81 family are endo-β(1,3)-glucanases ([{{EClink}}3.2.1.39 EC 3.2.1.39]) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in ''Saccharomyces'', and ''Streptomyces'' species. Activity has been demonstrated on laminarin <cite>Fontaine1997, McGrath2006, Martin-Cuadrado2008, Zhou2013, Pluvinage2017, Kumar2018</cite>, curdlan <cite>Fontaine1997, Martin-Cuadrado2008, Pluvinage2017, Kumar2018</cite>, and pachyman <cite>McGrath2006, Pluvinage2017</cite>. | GH81 family are endo-β(1,3)-glucanases ([{{EClink}}3.2.1.39 EC 3.2.1.39]) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in ''Saccharomyces'', and ''Streptomyces'' species. Activity has been demonstrated on laminarin <cite>Fontaine1997, McGrath2006, Martin-Cuadrado2008, Zhou2013, Pluvinage2017, Kumar2018</cite>, curdlan <cite>Fontaine1997, Martin-Cuadrado2008, Pluvinage2017, Kumar2018</cite>, and pachyman <cite>McGrath2006, Pluvinage2017</cite>. | ||
| + | |||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | + | GH81 enzymes follow an [[inverting]] mechanism, first shown by <sup>1</sup>H-NMR during the hydrolysis of laminarioligosaccharides <cite>Fliegmann2005</cite>, and laminarin <cite>McGrath2006</cite>, thus operating by a [[Glycoside_hydrolases#Inverting_glycoside_hydrolases|single-displacement mechanism]]. | |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 53: | Line 54: | ||
#Pluvinage2017 pmid=28781080 | #Pluvinage2017 pmid=28781080 | ||
#Kumar2018 pmid=29870811 | #Kumar2018 pmid=29870811 | ||
| + | #Fliegmann2005 pmid=16297387 | ||
| + | |||
</biblio> | </biblio> | ||
[[Category:Glycoside Hydrolase Families|GH081]] | [[Category:Glycoside Hydrolase Families|GH081]] | ||
Revision as of 12:56, 21 July 2020
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.
- Author: ^^^Julie Grondin^^^
- Responsible Curator: ^^^Al Boraston^^^
| Glycoside Hydrolase Family GH81 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH81.html | |
Substrate specificities
GH81 family are endo-β(1,3)-glucanases (EC 3.2.1.39) with diverse physiological roles, such as plant biomass degradation, cell cycling, and enzymatic pathogen defense. They are mostly found in bacteria and fungi, particularly abundant in Saccharomyces, and Streptomyces species. Activity has been demonstrated on laminarin [1, 2, 3, 4, 5, 6], curdlan [1, 3, 5, 6], and pachyman [2, 5].
Kinetics and Mechanism
GH81 enzymes follow an inverting mechanism, first shown by 1H-NMR during the hydrolysis of laminarioligosaccharides [7], and laminarin [2], thus operating by a single-displacement mechanism.
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
- Fontaine T, Hartland RP, Beauvais A, Diaquin M, and Latge JP. (1997). Purification and characterization of an endo-1,3-beta-glucanase from Aspergillus fumigatus. Eur J Biochem. 1997;243(1-2):315-21. DOI:10.1111/j.1432-1033.1997.0315a.x |
- McGrath CE and Wilson DB. (2006). Characterization of a Thermobifida fusca beta-1,3-glucanase (Lam81A) with a potential role in plant biomass degradation. Biochemistry. 2006;45(47):14094-100. DOI:10.1021/bi061757r |
- Martín-Cuadrado AB, Fontaine T, Esteban PF, del Dedo JE, de Medina-Redondo M, del Rey F, Latgé JP, and de Aldana CR. (2008). Characterization of the endo-beta-1,3-glucanase activity of S. cerevisiae Eng2 and other members of the GH81 family. Fungal Genet Biol. 2008;45(4):542-53. DOI:10.1016/j.fgb.2007.09.001 |
- Zhou P, Chen Z, Yan Q, Yang S, Hilgenfeld R, and Jiang Z. (2013). The structure of a glycoside hydrolase family 81 endo-β-1,3-glucanase. Acta Crystallogr D Biol Crystallogr. 2013;69(Pt 10):2027-38. DOI:10.1107/S090744491301799X |
- Pluvinage B, Fillo A, Massel P, and Boraston AB. (2017). Structural Analysis of a Family 81 Glycoside Hydrolase Implicates Its Recognition of β-1,3-Glucan Quaternary Structure. Structure. 2017;25(9):1348-1359.e3. DOI:10.1016/j.str.2017.06.019 |
- Kumar K, Correia MAS, Pires VMR, Dhillon A, Sharma K, Rajulapati V, Fontes CMGA, Carvalho AL, and Goyal A. (2018). Novel insights into the degradation of β-1,3-glucans by the cellulosome of Clostridium thermocellum revealed by structure and function studies of a family 81 glycoside hydrolase. Int J Biol Macromol. 2018;117:890-901. DOI:10.1016/j.ijbiomac.2018.06.003 |
- Fliegmann J, Montel E, Djulić A, Cottaz S, Driguez H, and Ebel J. (2005). Catalytic properties of the bifunctional soybean beta-glucan-binding protein, a member of family 81 glycoside hydrolases. FEBS Lett. 2005;579(29):6647-52. DOI:10.1016/j.febslet.2005.10.060 |