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] 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 .
Activity Regulation Classification Kinetics Types
