Glycoside Hydrolase Family 115

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Glycoside Hydrolase Family GH115
Clan none
Mechanism inverting
Active site residues not known
CAZy DB link
http://www.cazy.org/GH115.html


Contents

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

  1. Ryabova O, Vrsanská M, Kaneko S, van Zyl WH, and Biely P. A novel family of hemicellulolytic alpha-glucuronidase. FEBS Lett. 2009 May 6;583(9):1457-62. DOI:10.1016/j.febslet.2009.03.057 | PubMed ID:19344716 | HubMed [Ryabova2009]
  2. Khandke KM, Vithayathil PJ, and Murthy SK. Purification and characterization of an alpha-D-glucuronidase from a thermophilic fungus, Thermoascus aurantiacus. Arch Biochem Biophys. 1989 Nov 1;274(2):511-7. PubMed ID:2802623 | HubMed [Khandke1989]
  3. Tenkanen M and Siika-aho M. An alpha-glucuronidase of Schizophyllum commune acting on polymeric xylan. J Biotechnol. 2000 Mar 10;78(2):149-61. PubMed ID:10725538 | HubMed [Tenkanen2000]
  4. Chong SL, Battaglia E, Coutinho PM, Henrissat B, Tenkanen M, and 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):1323-32. DOI:10.1007/s00253-011-3157-y | PubMed ID:21442271 | HubMed [Chong2011]
  5. Fujimoto Z, Ichinose H, Biely P, and 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. DOI:10.1107/S1744309110043721 | PubMed ID:21206027 | HubMed [Fujimoto2011]
  6. Kolenová K, Ryabova O, Vrsanská M, and Biely P. Inverting character of family GH115 α-glucuronidases. FEBS Lett. 2010 Sep 24;584(18):4063-8. DOI:10.1016/j.febslet.2010.08.031 | PubMed ID:20804758 | HubMed [Kolenova2010]
All Medline abstracts: PubMed | HubMed
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