| Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | NAGLU | ||||||||
| Pfam | PF05089 | ||||||||
| Pfam clan | CL0058 | ||||||||
| InterPro | IPR007781 | ||||||||
| CAZy | GH89 | ||||||||
| |||||||||
| Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | NAGLU_N | ||||||||
| Pfam | PF12971 | ||||||||
| CAZy | GH89 | ||||||||
| |||||||||
| Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | NAGLU_C | ||||||||
| Pfam | PF12972 | ||||||||
| CAZy | GH89 | ||||||||
| |||||||||
In molecular biology, glycoside hydrolase family 89 is a family of glycoside hydrolases.
Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycoside hydrolases, based on sequence similarity, has led to the definition of >100 different families.[1][2][3] This classification is available on the CAZy web site,[4][5] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[6][7]
Glycoside hydrolase family 89 CAZY GH_89 includes enzymes with α-N-acetylglucosaminidase EC 3.2.1.50 activity. The enzyme consist of three structural domains, the N-terminal domain has an alpha-beta fold, the central domain has a TIM barrel fold, and the C-terminal domain has an all alpha helical fold.[8]
Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate.[9] Mutations on the alpha-N-acetylglucosaminidase (NAGLU) gene can lead to Mucopolysaccharidosis type IIIB (MPS IIIB; or Sanfilippo syndrome type B) characterised by neurological dysfunction but relatively mild somatic manifestations.[10]
References
- ↑ Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G (July 1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proceedings of the National Academy of Sciences of the United States of America. 92 (15): 7090–4. Bibcode:1995PNAS...92.7090H. doi:10.1073/pnas.92.15.7090. PMC 41477. PMID 7624375.
- ↑ Davies G, Henrissat B (September 1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–9. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
- ↑ Henrissat B, Bairoch A (June 1996). "Updating the sequence-based classification of glycosyl hydrolases". The Biochemical Journal. 316 (Pt 2): 695–6. doi:10.1042/bj3160695. PMC 1217404. PMID 8687420.
- ↑ "Home". CAZy.org. Retrieved 2018-03-06.
- ↑ Lombard V, Golaconda Ramulu H, Drula E, Coutinho PM, Henrissat B (January 2014). "The carbohydrate-active enzymes database (CAZy) in 2013". Nucleic Acids Research. 42 (Database issue): D490–5. doi:10.1093/nar/gkt1178. PMC 3965031. PMID 24270786.
- ↑ "Glycoside Hydrolase Family 89". CAZypedia.org. Retrieved 2018-03-06.
- ↑ CAZypedia Consortium (December 2018). "Ten years of CAZypedia: a living encyclopedia of carbohydrate-active enzymes" (PDF). Glycobiology. 28 (1): 3–8. doi:10.1093/glycob/cwx089. PMID 29040563.
- ↑ Ficko-Blean E, Stubbs KA, Nemirovsky O, Vocadlo DJ, Boraston AB (2008). "Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB". Proc Natl Acad Sci U S A. 105 (18): 6560–5. Bibcode:2008PNAS..105.6560F. doi:10.1073/pnas.0711491105. PMC 2373330. PMID 18443291.
- ↑ Li HH, Yu WH, Rozengurt N, Zhao HZ, Lyons KM, Anagnostaras S, Fanselow MS, Suzuki K, Vanier MT, Neufeld EF (December 1999). "Mouse model of Sanfilippo syndrome type B produced by targeted disruption of the gene encoding alpha-N-acetylglucosaminidase". Proc. Natl. Acad. Sci. U.S.A. 96 (25): 14505–10. Bibcode:1999PNAS...9614505L. doi:10.1073/pnas.96.25.14505. PMC 24466. PMID 10588735.
- ↑ Villani GR, Follenzi A, Vanacore B, Di Domenico C, Naldini L, Di Natale P (June 2002). "Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer". Biochem. J. 364 (Pt 3): 747–53. doi:10.1042/BJ20011872. PMC 1222624. PMID 12049639.