Glycoside hydrolase family 89

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(http://www.cazy.org/GH1.html) web site,[4] and also discussed at CAZypedia, an online encyclopedia of carbohydrate active enzymes.[5]

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.[6]

Alpha-N-acetylglucosaminidase is a lysosomal enzyme required for the stepwise degradation of heparan sulphate.[7] 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.[8]

References

  1. ↑ Henrissat B, Callebaut I, Mornon JP, Fabrega S, Lehn P, Davies G (1995). "Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 7090–7094. doi:10.1073/pnas.92.15.7090. PMC 41477Freely accessible. PMID 7624375.
  2. ↑ Henrissat B, Davies G (1995). "Structures and mechanisms of glycosyl hydrolases". Structure. 3 (9): 853–859. doi:10.1016/S0969-2126(01)00220-9. PMID 8535779.
  3. ↑ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999.
  4. ↑ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999.
  5. ↑ CAZypedia, an online encyclopedia of carbohydrate-active enzymes.
  6. ↑ 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. doi:10.1073/pnas.0711491105. PMC 2373330Freely accessible. PMID 18443291.
  7. ↑ 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. doi:10.1073/pnas.96.25.14505. PMC 24466Freely accessible. PMID 10588735.
  8. ↑ 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 1222624Freely accessible. PMID 12049639.

This article incorporates text from the public domain Pfam and InterPro IPR007781

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