Glycoside Hydrolase Family 89

• Author: ^^^Elizabeth Ficko-Blean^^^
• Responsible Curator: ^^^Alisdair Boraston^^^

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Glycoside Hydrolase Family GH89
Clan	none
Mechanism	Retaining
Active site residues	known
CAZy DB link
http://www.cazy.org/fam/GH89.html

Substrate specificities

The family 89 glycoside hydrolases are active as α-N-acetylglucosaminidases. The human lysosomal enzyme, NAGLU, is involved in the degradation of heparan sulfate. Mutations in this enzyme can cause a devastating disease called Sanfilippo syndrome type B which is also called mucopolysaccharidosis IIIB.

Kinetics and Mechanism

Mechanistic and structural data is available on CpGH89, a family 89 glycoside hydrolase produced by Clostridium perfringens. CpGH89 uses a double displacement mechanism to hydrolyze the glycosidic bond which results in retention of stereochemistry at the anomeric carbon.

Family Firsts

First sterochemistry determination

Cite some reference here, with a short explanation [1].

First catalytic nucleophile identification

First general acid/base residue identification

First 3-D structure

References

1. Ficko-Blean E, Stubbs KA, Nemirovsky O, Vocadlo DJ, and Boraston AB. (2008). Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB. Proc Natl Acad Sci U S A. 2008;105(18):6560-5. DOI:10.1073/pnas.0711491105 |