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Protein domain
Protein domain
Protein domain
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] CAZy web site,[ 4] [ 5] [ 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]
^ 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 .
Activity Regulation Classification Kinetics Types
