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Glycoside Hydrolase Family 115
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|Glycoside Hydrolase Family GH115|
|Active site residues||not known|
|CAZy DB link|
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 126.96.36.199). 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 . This substrate specificity was first demonstrated by an α-glucuronidase purified from Thermoascus aurantiacus , and later for a Schizophyllum commune α-glucuronidase . Although GH115 was established on the basis of biochemical and sequence analysis of Pichia stipitis (4-O-methyl)-α-glucuronidase , available N-terminal protein sequence of the S. commune enzyme  allowed the tentative assignment of this enzyme to GH115 , which was later confirmed by the full protein sequence . 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 .
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 .
The catalytic residues have not yet been identified in a member of this family.
No 3D structure has been solved for this family at present, although crystallization of a Streptomyces pristinaespiralis homolog has been reported .
- 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 .
- 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 .
- 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 |
- Chong SL, Battaglia E, Coutinho PM, Henrissat B, Tenkanen M, and de Vries RP. (2011). The α-glucuronidase Agu1 from Schizophyllum commune is a member of a novel glycoside hydrolase family (GH115). Appl Microbiol Biotechnol. 2011;90(4):1323-32. DOI:10.1007/s00253-011-3157-y |
- Fujimoto Z, Ichinose H, Biely P, and Kaneko S. (2011). 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;67(Pt 1):68-71. DOI:10.1107/S1744309110043721 |
- Kolenová K, Ryabova O, Vrsanská M, and Biely P. (2010). Inverting character of family GH115 α-glucuronidases. FEBS Lett. 2010;584(18):4063-8. DOI:10.1016/j.febslet.2010.08.031 |