Glycoside Hydrolase Family 17

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• Author: ^^^Geoff Fincher^^^
• Responsible Curator: ^^^Bernard Henrissat^^^

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

Substrate specificities

The family GH17 glycoside hydrolases are clan GH-A enzymes from bacteria, fungi and plants, and include two major groups of enzymes with related but distinct substrate specificities, namely (1,3)-beta-D-glucan endohydrolases (EC 3.1.2.39) and (1,3;1,4)-beta-D-glucan endohydrolases (EC 3.1.2.73). A (1,3)-beta-D-glucan exohydrolase (EC 3.1.2.58) is also classified in this family. The family 17 enzymes have quite distinct amino acid sequences and 3D structures compared with the (1,3)-beta-D-glucan endohydrolases and (1,3;1,4)-beta-D-glucan endohydrolases that have similar substrate specificities but are classified in families GH16, GH55, GH64 and GH81.

The family GH17 (1,3)-beta-D-glucan endohydrolases hydrolyse internal (1,3)-beta-D-glucosidic linkages in polysaccharides, but usually require a region of contiguous unbranched, un-substituted (1,3)-beta-D-glucosyl residues for activity. The enzymes release (1,3)-beta-D-oligoglucosides of DP 2-5 as their major products. Because the (1,3)-beta-D-glucan endohydrolases require a region of contiguous unbranched, un-substituted (1,3)-beta-D-glucosyl residues for activity, they are unable to hydrolyse the single (1,3)-beta-D-glucosidic linkages in (1,3;1,4)-beta-D-glucans from the Poaceae, but they will hydrolyse (1,3)-beta-D-glucosidic linkages in fungal (1,3;1,6)-beta-D-glucans, provided an appropriate region of contiguous un-substituted (1,3)-beta-D-glucosyl residues is available. The family GH17 (1,3;1,4)-beta-D-glucan endohydrolases (EC 3.1.2.73) hydrolyse (1,4)-beta-D-glucosidic linkages, but only (1,3;1,4)-beta-D-glucans in which the glucosyl residue involved in the glycosidic linkage cleaved is substituted at the C(0)3 position, that is, where the (1,4)-beta-D-glucosidic linkages are located on the reducing end side of (1,3)-beta-D-glucosyl residues.

  Normal  0      21      false  false  false    FR  X-NONE  X-NONE                                       MicrosoftInternetExplorer4                                                                                                                                                                                                                                                                                                                             Reaction products released are mainly (1,3;1,4)-beta-D-tri- and tetrasaccharides (G4G3Gred and G4G4G3Gred), but they also release higher oligosaccharides of up to 10 or more contiguous (1,4)-beta-D-glucosyl residues with a single reducing terminal (1,3)-beta-D-glucosyl residue (e.g. G4G4G4G4G4G4G3Gred).  These longer oligosaccharides originate from the longer regions of adjacent (1,4)-linkages that account for approximately 10% by weight of (1,3;1,4)-beta-D-glucans in cell walls of the Poaceae.  

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

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Catalytic Residues

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Three-dimensional structures

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Family Firsts

First sterochemistry determination

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First catalytic nucleophile identification

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First general acid/base residue identification

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First 3-D structure

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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 |

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