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Difference between revisions of "Glycoside Hydrolase Family 130"
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[[GH130]] contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), β-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. | [[GH130]] contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC [{{EClink}}2.4.1.281 2.4.1.281]), β-1,4-mannooligosaccharide phosphorylase(EC [{{EClink}}2.4.1.319 2.4.1.319]), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC [{{EClink}}2.4.1.320 2.4.1.320]) are members of this family. | ||
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | GH130 phosphorylases phosphorolyze β1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-β-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces α-mannose 1-phosphate and glucose from 4-O-β-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of ''B. fragilis'' 4-O-β-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, | + | GH130 phosphorylases phosphorolyze β1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. <cite>Senoura2011</cite> demonstrated that 4-O-β-D-Mannosyl-D-glucose phosphorylase from ''Bacteroides fragilis'' produces α-mannose 1-phosphate and glucose from 4-O-β-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of ''B. fragilis'' 4-O-β-D-Mannosyl-D-glucose phosphorylase <cite>Nakae2013</cite>. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in ''B. fragilis'' 4-O-β-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and α-mannose 1-phosphate is generated. |
== Catalytic Residues == | == Catalytic Residues == | ||
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Revision as of 18:34, 16 November 2014
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: ^^^Wataru Saburi^^^
- Responsible Curator: ^^^Haruhide Mori^^^
| Glycoside Hydrolase Family GH130 | |
| Clan | GH-x |
| Mechanism | retaining/inverting |
| Active site residues | known/not known |
| CAZy DB link | |
| https://www.cazy.org/GH130.html | |
Substrate specificities
GH130 contains phosphorylases catalyzing the phosphorolysis of β1-4mannosidic linkage at the non-reducing end of substrates. 4-O-β-D-Mannosyl-D-glucose phosphorylase (EC 2.4.1.281), β-1,4-mannooligosaccharide phosphorylase(EC 2.4.1.319), and 1,4-β-mannosyl-N-acetylglucosamine phosphorylase (EC 2.4.1.320) are members of this family.
Kinetics and Mechanism
GH130 phosphorylases phosphorolyze β1-4mannosidic linkage at the non-reducing end of substrates with net inversion of anomeric configuration. Senoura et al. [1] demonstrated that 4-O-β-D-Mannosyl-D-glucose phosphorylase from Bacteroides fragilis produces α-mannose 1-phosphate and glucose from 4-O-β-D-Mannosyl-D-glucose and inorganic phosphate. A unique reaction mechanism of GH130 enzymes has been proposed on the basis of the three-dimensional strucuture analysis of B. fragilis 4-O-β-D-Mannosyl-D-glucose phosphorylase [2]. In contrast to known inverting glycoside phosphorylases, whose general acid catalyst directly donates a proton to glycosidic oxygen, the catalytic Asp of GH130 enzymes (Asp131 in B. fragilis 4-O-β-D-Mannosyl-D-glucose phosphorylase) donates a proton to O3 of mannosyl group bond to subsite -1, and a proton is tranferred to the glycosidic oxygen from 3OH group of the mannosyl residue. Inorganic phosphate attacks C1 of the mannosyl residue at the non-reducing end of substrate and α-mannose 1-phosphate is generated.
Catalytic Residues
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Three-dimensional structures
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Family Firsts
- First stereochemistry determination
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- First catalytic nucleophile identification
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- First general acid/base residue identification
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- First 3-D structure
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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. Biochem. J. (BJ Classic Paper, online only). DOI: 10.1042/BJ20080382