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Difference between revisions of "Glycoside Hydrolase Family 89"
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== Substrate specificities == | == Substrate specificities == | ||
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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 or mucopolysaccharidosis IIIB. | 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 or mucopolysaccharidosis IIIB. | ||
Revision as of 10:23, 21 October 2009
- Author: ^^^Elizabeth Ficko-Blean^^^
- Responsible Curator: ^^^Alisdair Boraston^^^
| 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 or mucopolysaccharidosis IIIB.
Kinetics and Mechanism
Mechanistic and structural characterization is available on CpGH89, a family 89 glycoside hydrolase produced by Clostridium perfringens.
Catalytic Residues
Three-dimensional structures
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