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Difference between revisions of "Glycoside Hydrolase Family 115"
| Line 29: | Line 29: | ||
== Substrate specificities == | == Substrate specificities == | ||
| − | [[Glycoside hydrolases]] of GH115 display | + | [[Glycoside hydrolases]] of GH115 display α-glucuronidase activity. In particular, members of this family catalyze the cleavage of 4-''O''-methyl D-glucuronic acid sidechains from native xylan polysaccharides (EC [{{EClink}}3.2.1.131 3.2.1.131)]. In contrast to [[GH67]] enzymes, which only cleave glucuronosyl linkages at the non-reducing ends of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans <cite>Ryabova2009</cite>. This substrate specificity was first demonstrated by an α-glucuronidase purified from ''Thermoascus aurantiacus'' <cite>Khandke1989</cite>, and later for a ''Schizophyllum commune'' α-glucuronidase <cite>Tenkanen2000</cite>. Although GH115 was established on the basis of biochemical and sequence analysis of ''Pichia stipitis'' (4-''O''-methyl)-α-glucuronidase <cite>Ryabova2009</cite>, available N-terminal protein sequence of the ''S. commune'' enzyme <cite>Tenkanen2000</cite> allowed the tentative assignment of this enzyme to GH115 <cite>Ryabova2009</cite>, which was later confirmed by the full protein sequence <cite>Chong2011</cite>. A GH115 member from ''Streptomyces pristinaespiralis'' produces both 4-''O''-methyl-D-glucuronic acid and non-methylated D-glucuronic acid from xylan and xylo-oligosaccharides <cite>Fujimoto2011</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
| − | Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by <sup>1</sup>H-NMR spectroscopy revealed that the enzymes from both ''S. commune'' and ''P. stipitis'' release the | + | Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by <sup>1</sup>H-NMR spectroscopy revealed that the enzymes from both ''S. commune'' and ''P. stipitis'' release the β-anomer of 4-O-methyl-D-glucuronic acid (MeGlcA) as the first-formed product, thus suggesting a one step, [[inverting]] mechanism <cite>Kolenova2010</cite>. |
== Catalytic Residues == | == Catalytic Residues == | ||
| Line 41: | Line 41: | ||
== Family Firsts == | == Family Firsts == | ||
| − | ;First stereochemistry determination: Release of the | + | ;First stereochemistry determination: Release of the β-anomer of 4-methyl-D-glucuronic acid by both the ''Schizophyllum commune'' and ''Pichia stipitis'' enzymes using <sup>1</sup>H NMR <cite>Kolenova2010</cite>. |
;First [[general acid]] residue identification: Not yet identified. | ;First [[general acid]] residue identification: Not yet identified. | ||
;First [[general base]] residue identification: Not yet identified. | ;First [[general base]] residue identification: Not yet identified. | ||
Revision as of 17:24, 8 June 2011
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- Author: ^^^Satoshi Kaneko^^^
- Responsible Curator: ^^^Satoshi Kaneko^^^
| Glycoside Hydrolase Family GH115 | |
| Clan | none |
| Mechanism | inverting |
| Active site residues | not known |
| CAZy DB link | |
| https://www.cazy.org/GH115.html | |
Substrate specificities
Glycoside hydrolases of GH115 display α-glucuronidase activity. In particular, members of this family catalyze the cleavage of 4-O-methyl D-glucuronic acid sidechains from native xylan polysaccharides (EC 3.2.1.131). In contrast to GH67 enzymes, which only cleave glucuronosyl linkages at the non-reducing ends of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans [1]. This substrate specificity was first demonstrated by an α-glucuronidase purified from Thermoascus aurantiacus [2], and later for a Schizophyllum commune α-glucuronidase [3]. Although GH115 was established on the basis of biochemical and sequence analysis of Pichia stipitis (4-O-methyl)-α-glucuronidase [1], available N-terminal protein sequence of the S. commune enzyme [3] allowed the tentative assignment of this enzyme to GH115 [1], which was later confirmed by the full protein sequence [4]. A GH115 member from Streptomyces pristinaespiralis produces both 4-O-methyl-D-glucuronic acid and non-methylated D-glucuronic acid from xylan and xylo-oligosaccharides [5].
Kinetics and Mechanism
Using reduced aldopentauronic acid (MeGlcA3Xyl4-ol) as a substrate, analysis by 1H-NMR spectroscopy revealed that the enzymes from both S. commune and P. stipitis release the β-anomer of 4-O-methyl-D-glucuronic acid (MeGlcA) as the first-formed product, thus suggesting a one step, inverting mechanism [6].
Catalytic Residues
The catalytic residues have not yet been identified in a member of this family.
Three-dimensional structures
No 3D structure has been solved for this family at present, although crystallization of a Streptomyces pristinaespiralis homolog has been reported [5].
Family Firsts
- First stereochemistry determination
- Release of the β-anomer of 4-methyl-D-glucuronic acid by both the Schizophyllum commune and Pichia stipitis enzymes using 1H NMR [6].
- First general acid residue identification
- Not yet identified.
- First general base residue identification
- Not yet identified.
- First 3-D structure
- Crystallization of the Streptomyces pristinaespiralis family member has been reported [5].
References
- Ryabova O, Vrsanská M, Kaneko S, van Zyl WH, and Biely P. (2009). A novel family of hemicellulolytic alpha-glucuronidase. FEBS Lett. 2009;583(9):1457-62. DOI:10.1016/j.febslet.2009.03.057 |
- Khandke KM, Vithayathil PJ, and Murthy SK. (1989). Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus. Arch Biochem Biophys. 1989;274(2):511-7. DOI:10.1016/0003-9861(89)90464-5 |
- Tenkanen M and Siika-aho M. (2000). An alpha-glucuronidase of Schizophyllum commune acting on polymeric xylan. J Biotechnol. 2000;78(2):149-61. DOI:10.1016/s0168-1656(99)00240-0 |
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Chong SL, Battaglia E, Coutinho PM, Henrissat B, Tenkanen M, de Vries RP. The α-glucuronidase Agu1 from Schizophyllum commune is a member of a novel glycoside hydrolase family (GH115). Appl Microbiol Biotechnol. 2011 May;90(4):1323-1332.
Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out: DOI:10.1007/s00253-011-3157-y PMID: 21442271
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Fujimoto Z, Ichinose H, Biely P, Kaneko S. Crystallization and preliminary crystallographic analysis of the glycoside hydrolase family 115 α-glucuronidase from Streptomyces pristinaespiralis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):68-71.
Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out: DOI:10.1107/S1744309110043721 PMID: 21206027
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Kolenová K, Ryabova O, Vrsanská M, Biely P. Inverting character of family GH115 α-glucuronidases. FEBS Lett. 2010 Sep 24;584(18):4063-4068.
Note: Due to a problem with PubMed data, this reference is not automatically formatted. Please see these links out: DOI:10.1016/j.febslet.2010.08.031 PMID: 20804758