Difference between revisions of "Glycoside Hydrolase Family 115"

Latest revision as of 13:16, 18 December 2021

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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

Error fetching PMID 2802623:
Error fetching PMID 10725538:
Error fetching PMID 19344716:
Error fetching PMID 20804758:
Error fetching PMID 21206027:
Error fetching PMID 21442271:

Error fetching PMID 19344716: [Ryabova2009]
Error fetching PMID 2802623: [Khandke1989]
Error fetching PMID 10725538: [Tenkanen2000]
Error fetching PMID 21442271: [Chong2011]
Error fetching PMID 21206027: [Fujimoto2011]
Error fetching PMID 20804758: [Kolenova2010]

All Medline abstracts: PubMed

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-* [[Author]]: ^^^Satoshi Kaneko^^^
+* [[Author]]: [[User:Satoshi Kaneko|Satoshi Kaneko]]
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+* [[Responsible Curator]]:  [[User:Satoshi Kaneko|Satoshi Kaneko]]
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 |-
 |'''Clan'''
-|GH-x
+|none
 |-
 |'''Mechanism'''
-|retaining/inverting
+|inverting
 |-
 |'''Active site residues'''
-|known/not known
+|not known
 |-
 |{{Hl2}} colspan="2" align="center" |'''CAZy DB link'''
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 == Substrate specificities ==
-Content is to be added here.
+[[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>.
-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 ==
-Content is to be added here.
+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 ==
-Content is to be added here.
+The catalytic residues have not yet been identified in a member of this family.
 == Three-dimensional structures ==
-Content is to be added here.
+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 ==
-;First stereochemistry determination: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Comfort2007</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: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>Sinnott1990</cite>.
+;First [[general acid]] residue identification: Not yet identified.
-;First general acid/base residue identification: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>He1999</cite>.
+;First [[general base]] residue identification: Not yet identified.
-;First 3-D structure: Cite some reference here, with a ''short'' (1-2 sentence) explanation <cite>StickWilliams</cite>.
+;First 3-D structure: Crystallization of the ''Streptomyces pristinaespiralis'' family member has been reported <cite>Fujimoto2011</cite>.
 == References ==
 <biblio>
-#Comfort2007 pmid=17323919
+#Khandke1989 pmid=2802623
-#He1999 pmid=9312086
+#Tenkanen2000 pmid=10725538
-#StickWilliams isbn=978-0-240-52118-3
+#Ryabova2009 pmid=19344716
-#Sinnott1990 Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. [http://dx.doi.org/10.1021/cr00105a006 DOI: 10.1021/cr00105a006]
+#Kolenova2010 pmid=20804758
+#Fujimoto2011 pmid=21206027
+#Chong2011 pmid=21442271
 </biblio>
 [[Category:Glycoside Hydrolase Families|GH115]]