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Difference between revisions of "Glycoside Hydrolase Family 115"

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* [[Author]]: ^^^Satoshi Kaneko^^^
 
* [[Author]]: ^^^Satoshi Kaneko^^^
 
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* [[Responsible Curator]]:  ^^^Satoshi Kaneko^^^
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== Substrate specificities ==
 
== Substrate specificities ==
−
Glycoside hydrolases of this family display alpha-glucuronidase activity. The enzymes possible to release 4-O-methyl D-glucuronic acid from polymeric xylans. The substrate specificity could be distinguished from GH67 enzymes. In contrast to GH67 enzymes which only cleave glucuronosyl linkage at the non-reducing end of xylooligosaccharides, GH115 enzymes remove glucuronic acid from the both terminal and internal regions of xylooligosaccharides and xylans. This kind of substrate specificty firstly demonstrated by an alpha-glucuronidase purified from Thermoascus aurantiacus <cite>Khandke1989</cite> and N-terminal amino acid sequence of Schizophyllum commune firstly provided <cite>2</cite>. In spite of the N-terminal amino acid sequence of Pichia stipitis did not show significant similarity with the sequence of S. commune, the information lead to find full amino acid sequence and establish this family <cite>3</cite>. It has been demonstrated that these enzymes release 4-O-methyl D-glucuronic acid, the enzyme from Streptomyces pristinaespiralis produced the both 4-O-methyl D-glucuronic acid and non methylated D-glucuronic acid as the reaction product <cite>4</cite>.
+
[[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>.
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This is an example of how to make references to a journal article <cite>Comfort2007</cite>. (See the References section below).  Multiple references can go in the same place like this <cite>Comfort2007 He1999</cite>.  You can even cite books using just the ISBN <cite>StickWilliams</cite>.  References that are not in PubMed can be typed in by hand <cite>Sinnott1990</cite>.
 
−
 
 
  
 
== Kinetics and Mechanism ==
 
== Kinetics and Mechanism ==
−
Using 1H NMR spectroscopy and reduced aldopentaouronic acid(MeGlcA3Xyl4-ol) as a substrate, it was demonstrated that both the enzymes from S. commune and P. stipitis releasing 4-O-methyl-D-glucuronic acid (MeGlcA) as its beta-anomer, suggesting a single displacement mechanism [5].
+
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 ==
−
Not identified.
+
The catalytic residues have not yet been identified in a member of this family.
−
 
 
  
 
== Three-dimensional structures ==
 
== Three-dimensional structures ==
−
No 3D-structure is solved for this family of enzyme.
+
No 3D structure has been solved for this family at present, although crystallization of a ''Streptomyces pristinaespiralis'' homolog has been reported <cite>Fujimoto2011</cite>.
−
 
 
  
 
== Family Firsts ==
 
== Family Firsts ==
−
;   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      First stereochemistry determination:1H NMR demonstrated that the released 4-methyl-D-glucuronic acid was a beta anomer and thus that the enzyme is an inverter <cite>Kolenová2010</cite>.
+
;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 catalytic nucleophile identification:unproved.
+
;First [[general acid]] residue identification: Not yet identified.
−
;First general acid/base residue identification:unproved.
+
;First [[general base]] residue identification: Not yet identified.
−
;First 3-D structure:Just crystallization of S. pristinaespiralis enzyme is reported <cite>Fujimoto2011</cite>.
+
;First 3-D structure: Crystallization of the ''Streptomyces pristinaespiralis'' family member has been reported <cite>Fujimoto2011</cite>.
  
 
== References ==
 
== References ==
 
<biblio>
 
<biblio>
−
#Khandke1989 pmid=2082623
+
#Khandke1989 pmid=2802623
−
#   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      Tenkanen2000 pmid=   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      10725538
+
#Tenkanen2000 pmid=10725538
−
#   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      Ryabova2009 pmid=   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      19344716
+
#Ryabova2009 pmid=19344716
−
#   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      Fujimoto2011 pmid=   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      21206027
+
#Kolenova2010 pmid=20804758
−
#   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      Kolenová2010 pmid=   Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                      20804758
+
#Fujimoto2011 pmid=21206027
 +
#Chong2011 pmid=21442271
 
</biblio>
 
</biblio>
 +
  
 
[[Category:Glycoside Hydrolase Families|GH115]]
 
[[Category:Glycoside Hydrolase Families|GH115]]

Revision as of 15:28, 21 June 2012

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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


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. (2009). A novel family of hemicellulolytic alpha-glucuronidase. FEBS Lett. 2009;583(9):1457-62. DOI:10.1016/j.febslet.2009.03.057 | PubMed ID:19344716 [Ryabova2009]
  2. 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 | PubMed ID:2802623 [Khandke1989]
  3. 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 | PubMed ID:10725538 [Tenkanen2000]
  4. 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 | PubMed ID:21442271 [Chong2011]
  5. 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 | PubMed ID:21206027 [Fujimoto2011]
  6. 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 | PubMed ID:20804758 [Kolenova2010]

All Medline abstracts: PubMed

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