Glycoside hydrolase family 89

In molecular biology, glycoside hydrolase family 89 is a family of glycoside hydrolases.

Alpha-N-acetylglucosaminidase (NAGLU) tim-barrel domain
Identifiers
SymbolNAGLU
PfamPF05089
Pfam clanCL0058
InterProIPR007781
CAZyGH89
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Alpha-N-acetylglucosaminidase (NAGLU) N-terminal domain
Identifiers
SymbolNAGLU_N
PfamPF12971
CAZyGH89
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Alpha-N-acetylglucosaminidase (NAGLU) C-terminal domain
Identifiers
SymbolNAGLU_C
PfamPF12972
CAZyGH89
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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

  1. 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.
  2. 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.
  3. 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.
  4. "Home". CAZy.org. Retrieved 2018-03-06.
  5. 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.
  6. "Glycoside Hydrolase Family 89". CAZypedia.org. Retrieved 2018-03-06.
  7. 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.
  8. 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.
  9. 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.
  10. 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.
This article incorporates text from the public domain Pfam and InterPro: IPR007781
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