Glycoside Hydrolase Family 115

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• Author: ^^^Satoshi Kaneko^^^
• Responsible Curator: ^^^Satoshi Kaneko^^^

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Glycoside Hydrolase Family GH115
Clan	GH-x
Mechanism	inverting
Active site residues	not known
CAZy DB link
http://www.cazy.org/GH115.html

Substrate specificities

  Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                       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 [1] and N-terminal amino acid sequence of Schizophyllum commune firstly provided [2]. 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 [3]. 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 [4].

This is an example of how to make references to a journal article [1]. (See the References section below). Multiple references can go in the same place like this [1, 2]. You can even cite books using just the ISBN [3]. References that are not in PubMed can be typed in by hand [4].

Kinetics and Mechanism

  Normal  0          0  2    false  false  false    EN-US  JA  X-NONE

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].

Catalytic Residues

  Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                       Not identified.

Three-dimensional structures

  Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                       No 3D-structure is solved for this family of enzyme.

Family Firsts

  Normal  0          0  2    false  false  false    EN-US  JA  X-NONE                                                                                                                                                                                                                                                                                                                                                                                       1H NMR demonstrated that the released 4-methyl-D-glucuronic acid was a beta anomer and thus that the enzyme is an inverter [5]. [1].

First catalytic nucleophile identification

Normal 0 0 2 false false false EN-US JA X-NONE unproved [4].

First general acid/base residue identification

Normal 0 0 2 false false false EN-US JA X-NONE unproved [2].

First 3-D structure

Normal 0 0 2 false false false EN-US JA X-NONE Just crystallization of S. pristinaespiralis enzyme is reported [4]. [3].

References

1. Comfort DA, Bobrov KS, Ivanen DR, Shabalin KA, Harris JM, Kulminskaya AA, Brumer H, and Kelly RM. (2007). Biochemical analysis of Thermotoga maritima GH36 alpha-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry. 2007;46(11):3319-30. DOI:10.1021/bi061521n |
2. He S and Withers SG. (1997). Assignment of sweet almond beta-glucosidase as a family 1 glycosidase and identification of its active site nucleophile. J Biol Chem. 1997;272(40):24864-7. DOI:10.1074/jbc.272.40.24864 |
3. Robert V. Stick and Spencer J. Williams. (2009) Carbohydrates. Elsevier Science.

4. Sinnott, M.L. (1990) Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90, 1171-1202. DOI: 10.1021/cr00105a006