Glycoside Hydrolase Family 107

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• Author: ^^^David Teze^^^
• Responsible Curator: ^^^Al Boraston^^^

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Glycoside Hydrolase Family GH107
Clan	GH-R
Mechanism	retaining
Active site residues	known
CAZy DB link
https://www.cazy.org/GH107.html

Substrate specificities

The glycoside hydrolases of this family are endo-acting α-fucosidases active on sulfated fucans (or fucoidans) from brown algae.

All described GH107 family members are endo-1,4-fucanase of bacterial origin.

With enzymes from the CAZY family GH29 they form the clan GH-R.

Kinetics and Mechanism

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Catalytic Residues

The catalytic nucleophile is an aspartate, while the catalytic acid-base is a histidine. The later is unusual in GHs, and a divergence from GH29, but is likely necessary to avoid electronic repulsion with the substrate sulfate groups.

Three-dimensional structures

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Family Firsts

First stereochemistry 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. Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, and Henrissat B. (2009). The Carbohydrate-Active EnZymes database (CAZy): an expert resource for Glycogenomics. Nucleic Acids Res. 2009;37(Database issue):D233-8. DOI:10.1093/nar/gkn663 |

2. Davies, G.J. and Sinnott, M.L. (2008) Sorting the diverse: the sequence-based classifications of carbohydrate-active enzymes. The Biochemist, vol. 30, no. 4., pp. 26-32. Download PDF version.