From Wikipedia, the free encyclopedia
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] http://www.cazy.org/GH1.html ) web site,[ 4] [ 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
^ 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 41477 PMID 7624375 . ^ 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 . ^ Bairoch, A. "Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT". 1999. ^ Henrissat, B. and Coutinho P.M. "Carbohydrate-Active Enzymes server". 1999. ^ CAZypedia, an online encyclopedia of carbohydrate-active enzymes. ^ 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 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. 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 .
Activity Regulation Classification Kinetics Types
