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Information on EC 3.2.1.50 - alpha-N-acetylglucosaminidase and Organism(s) Homo sapiens and UniProt Accession P54802
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3.2.1.50 alpha-N-acetylglucosaminidaseIUBMB Comments
Hydrolyses UDP-N-acetylglucosamine.
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Word Map
- 3.2.1.50
- oligosaccharide
- glycoside
- lysosomal
- glycans
-
n-linked
- lectin
- beta-glucosidase
-
sialic
- neuraminidase
- glycoconjugates
- n-acetylglucosamine
-
iminosugars
- glycopeptides
-
sialylated
- glcnac
- alpha-l-fucosidase
- mucopolysaccharidosis
- sialidase
-
anomeric
-
polyhydroxylated
- swainsonine
-
mannosidase
- 1-deoxynojirimycin
-
asparagine-linked
-
fucosylated
-
high-mannose
- beta-n-acetylglucosaminidase
- beta-d-galactosidase
- naglu
-
complex-type
- alpha-d-mannosidase
- 1-deoxymannojirimycin
-
fucosidase
- alpha-d-galactosidase
-
n-acetyl-beta-d-glucosaminidase
- almond
-
transglycosylation
-
pngase
-
hydrazinolysis
- castanospermine
-
sulfonium
- alpha-n-acetylgalactosaminidase
- beta-d-xylosidase
- neuac
-
mannose-type
-
triantennary
- endo-beta-galactosidase
- beta-mannosidase
- alpha-d-glucosidase
- alpha-l-iduronidase
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
glycosidase, alpha-n-acetylglucosaminidase, exo-glycosidase, n-acetyl-alpha-d-glucosaminidase, heparan n-sulfatase, bmn 250, n-acetyl-alpha-glucosaminidase, alpha-acetylglucosaminidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BMN 250
tralesinidase alfa, a fusion protein of lysosomal alpha-N-acetylglucosaminidase with insulin-like growth factor 2
NAG
NAG
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
alpha-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase
Hydrolyses UDP-N-acetylglucosamine.
CAS REGISTRY NUMBER
COMMENTARY
37288-40-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl N-acetyl-alpha-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-alpha-D-glucosamine
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
4-methylumbelliferyl 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
?
-
-
-
?
4-methylumbelliferyl-2-acetamide-2-deoxy-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + 2-acetamide-2-deoxy-alpha-D-glucopyranose
-
-
-
-
?
methylumbelliferyl-N-acetyl-alpha-D-glucosaminide + H2O
methylumbelliferone + N-acetyl-alpha-D-glucosamine
O-(alpha-acetamido-2-deoxy-D-glucopyranosyl)-(1-3)-[L-6,3H]idoronic acid + H2O
?
-
-
-
?
o-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
o-nitrophenol + N-acetyl-alpha-D-glucosamine
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
UDP-N-acetyl-alpha-D-glucosamine + H2O
uridine-5'-diphosphate + N-acetyl-alpha-D-glucosamine
-
-
-
-
?
uridine-5'-diphospho-N-acetyl-alpha-D-glucosamine
uridine-5'-diphosphate + N-acetyl-alpha-D-glucosamine
4-methylumbelliferyl N-acetyl-alpha-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-alpha-D-glucosamine
-
-
-
?
4-methylumbelliferyl N-acetyl-alpha-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-alpha-D-glucosamine
-
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
-
?
methylumbelliferyl-N-acetyl-alpha-D-glucosaminide + H2O
methylumbelliferone + N-acetyl-alpha-D-glucosamine
-
-
-
?
methylumbelliferyl-N-acetyl-alpha-D-glucosaminide + H2O
methylumbelliferone + N-acetyl-alpha-D-glucosamine
-
-
-
?
o-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
o-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
o-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
o-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
p-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
p-nitrophenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
phenyl-N-acetyl-alpha-D-glucosaminide + H2O
phenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
phenyl-N-acetyl-alpha-D-glucosaminide + H2O
phenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
phenyl-N-acetyl-alpha-D-glucosaminide + H2O
phenol + N-acetyl-alpha-D-glucosamine
-
-
-
-
?
phenyl-N-acetyl-alpha-D-glucosaminide + H2O
phenol + N-acetyl-alpha-D-glucosamine
-
-
-
?
uridine-5'-diphospho-N-acetyl-alpha-D-glucosamine
uridine-5'-diphosphate + N-acetyl-alpha-D-glucosamine
-
-
-
?
uridine-5'-diphospho-N-acetyl-alpha-D-glucosamine
uridine-5'-diphosphate + N-acetyl-alpha-D-glucosamine
-
-
-
?
uridine-5'-diphospho-N-acetyl-alpha-D-glucosamine
uridine-5'-diphosphate + N-acetyl-alpha-D-glucosamine
-
-
-
?
additional information
?
-
-
mucopolysaccharidosis type IIIB is a lysosomal storage disorder characterized by the defective degradation of heparan sulfate due to a deficiency of alpha-N-acetylglucosaminidase. The clinical severity of mucopolysacchariddosis type IIIB ranges from an attenuated to severely affected Sanfilippo phenotype. Relationship between genotype, cellular biochemistry and clinical phenotype in a F48L/R297X compound heterozygous mucopolysaccharidosis type IIIB patient with an attenuated Sanfilippo phenotype
-
?
additional information
?
-
-
enzyme deficiency causes the Sanfilippo type B syndrome, i.e. the mucopolysaccharidosis type IIIB, a lysosomal storage disorder, phenotype, overview
-
-
?
additional information
?
-
-
enzyme deficiency causes the Sanfilippo type B syndrome, i.e. the mucopolysaccharidosis type IIIB, an autosomal recessive lysosomal storage disorder, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
?
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
involved in the degradation of heparin and heparan sulfate
-
-
?
additional information
?
-
-
mucopolysaccharidosis type IIIB is a lysosomal storage disorder characterized by the defective degradation of heparan sulfate due to a deficiency of alpha-N-acetylglucosaminidase. The clinical severity of mucopolysacchariddosis type IIIB ranges from an attenuated to severely affected Sanfilippo phenotype. Relationship between genotype, cellular biochemistry and clinical phenotype in a F48L/R297X compound heterozygous mucopolysaccharidosis type IIIB patient with an attenuated Sanfilippo phenotype
-
?
additional information
?
-
-
enzyme deficiency causes the Sanfilippo type B syndrome, i.e. the mucopolysaccharidosis type IIIB, a lysosomal storage disorder, phenotype, overview
-
-
?
additional information
?
-
-
enzyme deficiency causes the Sanfilippo type B syndrome, i.e. the mucopolysaccharidosis type IIIB, an autosomal recessive lysosomal storage disorder, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Hg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dermatan sulfate
-
competitive inhibition at 1 mM with p-nitrophenyl-alpha-N-acetylglucosaminide and UDP-N-acetylglucosamine as substrates
mouse anti-serum
-
raised in BALB/c mice, complete inhibition at pH 7.5
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
stabilization and acceleration of activity betweeen 0.05-0.1%, 2-3fold activity at 0.025%
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0166
O-(alpha-acetamido-2-deoxy-D-glucopyranosyl)-(1-3)-[L-6,3H]idoronic acid
-
pH 4.5, 37°C, with bovine serum albumin
0.043 - 0.61
o-nitrophenyl-alpha-N-acetylglucosaminide
-
0.23-0.25 in the presence of 0.025% bovine serum albumin
0.39
UDP-N-acetylglucosamine
-
0.58 in the presence of 0.025% bovine serum albumin
1.07
4-methylumbelliferyl 2-acetamido-2-deoxy-alpha-D-glucopyranoside
-
pH 4.5, 37°C, without bovine serum albumin
5.34
4-methylumbelliferyl 2-acetamido-2-deoxy-alpha-D-glucopyranoside
-
pH 4.5, 37°C, with bovine serum albumin
0.13 - 0.2
p-nitrophenyl-alpha-N-acetylglucosaminide
-
0.21-0.55 in the presence of 0.025% bovine serum albumin
0.12 - 1.6
phenyl-alpha-N-acetylglucosaminide
-
0.46-0.66 in the presence of 0.025% bovine serum albumin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.115 - 1.2
-
purified enzyme, p-nitrophenyl-N-acetyl-alpha-D-glucosaminide as substrate
0.58
-
purified enzyme, methylumbelliferyl-N-acetyl-alpha-D-glucosaminide as substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
4.5
4.6
4.8
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
malfunction
-
a large homozygous intragenic deletion in the alpha-N-acetylglucosaminidase gene, causing enzyme deficiency, is involved in the autosomal recessive disease Sanfilippo type B syndrome, i.e. mucopolysaccharidosis IIIB, in an affected child of consanguineous parents
malfunction
alpha-N-acetylglucosaminidase is a key enzyme in the pathogenesis of Sanfilippo syndrome B
malfunction
enzyme mutations cause the Sanfilippo B syndrome which leads to severe neurodegenerative disease and early death
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ANAG_HUMAN
743
0
82266
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
79000
-
x * 79000, two isoforms of recombinant enzyme with MW of 89000 Da and 79000 Da differ in their glycosylation pattern, SDS-PAGE
89000
-
x * 89000, two isoforms of recombinant enzyme with MW of 89000 Da and 79000 Da differ in their glycosylation pattern, SDS-PAGE
90000 - 180000
-
monomer of 90000 and dimer of 180000 in the ratio 1:2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
-
x * 79000, two isoforms of recombinant enzyme with MW of 89000 Da and 79000 Da differ in their glycosylation pattern, SDS-PAGE
?
-
x * 89000, two isoforms of recombinant enzyme with MW of 89000 Da and 79000 Da differ in their glycosylation pattern, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
the enzyme has 6 putative N-glycosylation sites at N261, N272, N435, N503, N526 and N532
glycoprotein
phosphoprotein
-
the specific phosphorylation of recombinant enzyme secreted from transfected CHO cells is significantly lower when compared with a control lysosomal enzyme
glycoprotein
-
two isoforms of recombinant enzyme with MW of 89000 Da and 79000 Da differ in their glycosylation pattern
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.01 M nickel chloride, 0.1M Tris (pH 8.5), 1.0 M lithium sulfate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R565P
-
naturally occurring mutation, five patients with the homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan show the Sanfilippo type B syndrome, heterozygotes show no phenotype
additional information
additional information
expression of human NaGlu in the central nervous system of mucopolysaccharidosis IIIB mice by an i.c. injection approach
additional information
-
expression of human NaGlu in the central nervous system of mucopolysaccharidosis IIIB mice by an i.c. injection approach
additional information
-
NAGLU-encoding gene: geneotyping and identification of a large homozygous intragenic deletion mutation in the alpha-N-acetylglucosaminidase gene, causing enzyme deficiency, involved in the autosomal recessive disease Sanfilippo type B syndrome, i.e. mucopolysaccharidosis IIIB, in a Turkish patient, phenotype,overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
5 - 9
-
no loss of activity by dialysis against 100 mM NaCl for 16 h, rapid loss of activity below pH 4 and above pH 10
208679
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 50
-
stable at 0°C and 23°C for 24 h, at 37°C loss of 45%, at 50°C loss of 85% of activity
50 - 70
50 - 70
-
no effect by 50°C heating, 50% inactivation after 12 min at 60°C and 2 min at 70°C
50 - 70
-
stable at 50°C for 1 h, at 55°C loss of 17%, at 60°C loss of 77% of activity
50 - 70
-
thermal stability increased after complex formation with rabbit antiserum
50 - 70
-
90% loss of activity after heating at 60°C for 10 min in the presence of 0.5% bovine serum albumin
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no proteolysis with pronase, bromelain and trypsin, 15% loss of activity after 30 min incubation with papain
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidation by periodate causes loss of 28% of activity after treatment with 10 mM at 4°C for 240 min
-
208681
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.9% NaCl, cultivated cells centrifuged at 1500 * g, 2 weeks, no loss of activity
-
4°C, 10 mM sodium phosphate buffer, pH 7.2, 150 mM NaCl, 1 year, no significant loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Sepharose 4 column chromatography and Q-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of Sanfilippo type B syndrome patients
-
expression of active alpha-N-acetylglucosaminidase/TAT chimerae in cultured Spodoptera frugiperda cells, establishment of an expression method for optimization of scale-up
-
NAGLU-encoding gene, located on chromosome 17q21.1, DNA and amino acid sequence determination and analysis, genotyping
-
R297X and F48L mutant alleles are engineered into the wild-type alpha-N-acetylglucosaminidase and expressed in Chinese hamster ovary cells. Wild-type enzyme and F48L mutant alleles are retrovirally expressed in mucopolysaccharidosis type IIIB skin fibroblasts
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
medicine
expression of human NaGlu in the central nervous system of mucopolysaccharidosis IIIB mice by an i.c. injection approach. The treatment slows the disease progression by mediating widespread recombinant NaGlu expression in the central nervous system, resulting in the reduction of brain lysosomal storage pathology, significantly improved cognitive function and prolonged survival. The therapeutic benefit of i.c. recombinant adeno-associated viral vector delivery is dose-dependent and can be attribute solely to the central nervous system transduction because the procedure does not lead to detectable transduction in somatic tissues
medicine
a minimum threshold of about 20% of wild type residual enzyme activity levels is required to completely prevent accumulation of heparan sulfate in Sanfilippo syndrome type B patient fibroblasts. BMN 250 cellular uptake under very limiting and transient exposure conditions occurs in sufficient amounts to reach this threshold
medicine
-
the use of secreted enzyme in future enzyme and gene replacement therapy protocols will by severely limited due to its small degree of mannose-6-phosphorylation
medicine
-
the enzyme is a possible candidate for enzyme replacement therapy, a method for cell entry or transduction has to be found
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Salvatore, D.; Bonatti, S.; Di Natale, P.
Lysosomal alpha-N-acetylglucosamidase: purification and characterization of the human urinary enzyme
Bull. Mol. Biol. Med.
9
111-121
1984
Homo sapiens
-
Roehrborn, W.; von Figura, K.
Human placenta alpha-N-acetylglucosaminidase: purification, characterization and demonstration of multiple recognition forms
Hoppe-Seyler's Z. Physiol. Chem.
359
1353-1362
1978
Homo sapiens
von Figura, K.
Human alpha-N-acetylglucosaminidase. 1. Purification and properties
Eur. J. Biochem.
80
525-533
1977
Homo sapiens
-
von Figura, K.
Human alpha-N-acetylglucosaminidase. 2. Activity towards natural substrates and multiple recognition forms
Eur. J. Biochem.
80
535-542
1977
Homo sapiens
Hultberg, B.; Lindsten, J.; Sjblad, S.
Molecular forms and activities of glycosidases in cultures of amniotic-fluid cells
Biochem. J.
155
599-605
1976
Homo sapiens
von Figura, K.; Kresse, H.
Sanfilippo disease type B: presence of material cross reacting with antibodies against alpha-N-acetylglucosaminidase
Eur. J. Biochem.
61
581-588
1976
Homo sapiens
Sasaki, T.; Sukegawa, K.; Masue, M.; Fukuda, S.; Tomatsu, S.; Orii, T.
Purification and partial characterization of alpha-N-acetylglucosaminidase from human liver
J. Biochem.
110
842-846
1991
Homo sapiens
Sasaki, T.; Sukegawa, K.; Masue, M.; Fukuda, S.; Tomatsu, S.; Inoue, N.; Orii, T.
Mucopolysaccharidosis type III B: Purification of alpha-N-acetylglucosaminidase from human liver
Connect. Tissue Res.
23
156-157
1992
Homo sapiens
-
Den Tandt, W.R.; Scharpe, S.
Micromethod determination of N-acetyl-alpha-D-glucosaminidase in human leukocytes and study of some of its characteristics
Int. J. Biochem.
25
209-212
1993
Homo sapiens
Zhao, Z.; Yazdani, A.; Shen, Y.; Sun, Z.S.; Bailey, J.; Caskey, C.T.; Lee, C.C.
Molecular dissection of a cosmid gene from a gene-rich region in 17q21 and characterization of a candidate gene for alpha-N-acetylglucosaminidase with two cDNA isoforms
Mamm. Genome
7
686-690
1996
Homo sapiens
Zhao, K.W.; Neufeld, E.F.
Purification and characterization of recombinant human alpha-N-acetylglucosaminidase secreted by chinese hamster ovary cells
Protein Expr. Purif.
19
202-211
2000
Homo sapiens
Yogalingam, G.; Weber, B.; Meehan, J.; Rogers, J.; Hopwood, J.J.
Mucopolysaccharidosis type IIIB: characterisation and expression of wild-type and mutant recombinant alpha-N-acetylglucosaminidase and relationship with sanfilippo phenotype in an attenuated patient
Biochim. Biophys. Acta
1502
415-425
2000
Homo sapiens
Weber, B.; Hopwood, J.J.; Yogalingam, G.
Expression and characterization of human recombinant and alpha-N-acetylglucosaminidase
Protein Expr. Purif.
21
251-259
2001
Homo sapiens
Chinen, Y.; Tohma, T.; Izumikawa, Y.; Uehara, H.; Ohta, T.
Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan
J. Hum. Genet.
50
357-359
2005
Homo sapiens
Bandsmer, J.C.; Campbell, T.N.; Cheyne, I.; Choy, F.Y.
Expression of active alpha-N-acetylglucosaminidase/TAT chimerae in cultured Spodoptera frugiperda cells
Protein Pept. Lett.
13
353-356
2006
Homo sapiens
Civallero, G.; Michelin, K.; de Mari, J.; Viapiana, M.; Burin, M.; Coelho, J.C.; Giugliani, R.
Twelve different enzyme assays on dried-blood filter paper samples for detection of patients with selected inherited lysosomal storage diseases
Clin. Chim. Acta
372
98-102
2006
Homo sapiens
Mangas, M.; Nogueira, C.; Prata, M.J.; Lacerda, L.; Coll, M.J.; Soares, G.; Ribeiro, G.; Amaral, O.; Ferreira, C.; Alves, C.; Coutinho, M.F.; Alves, S.
Molecular analysis of mucopolysaccharidosis type IIIB in Portugal: evidence of a single origin for a common mutation (R234C) in the Iberian Peninsula
Clin. Genet.
73
251-256
2008
Homo sapiens
Champion, K.J.; Basehore, M.J.; Wood, T.; Destree, A.; Vannuffel, P.; Maystadt, I.
Identification and characterization of a novel homozygous deletion in the alpha-N-acetylglucosaminidase gene in a patient with Sanfilippo type B syndrome (mucopolysaccharidosis IIIB)
Mol. Genet. Metab.
100
51-56
2010
Homo sapiens
Fu, H.; DiRosario, J.; Kang, L.; Muenzer, J.; McCarty, D.M.
Restoration of central nervous system alpha-N-acetylglucosaminidase activity and therapeutic benefits in mucopolysaccharidosis IIIB mice by a single intracisternal recombinant adeno-associated viral type 2 vector delivery
J. Gene Med.
12
624-633
2010
Homo sapiens (P54802), Homo sapiens
Birrane, G.; Dassier, A.L.; Romashko, A.; Lundberg, D.; Holmes, K.; Cottle, T.; Norton, A.W.; Zhang, B.; Concino, M.F.; Meiyappan, M.
Structural characterization of the alpha-N-acetylglucosaminidase, a key enzyme in the pathogenesis of Sanfilippo syndrome B
J. Struct. Biol.
205
65-71
2019
Homo sapiens (P54802), Homo sapiens
Yogalingam, G.; Luu, A.R.; Prill, H.; Lo, M.J.; Yip, B.; Holtzinger, J.; Christianson, T.; Aoyagi-Scharber, M.; Lawrence, R.; Crawford, B.E.; LeBowitz, J.H.
BMN 250, a fusion of lysosomal alpha-N-acetylglucosaminidase with IGF2, exhibits different patterns of cellular uptake into critical cell types of Sanfilippo syndrome B disease pathogenesis
PLoS ONE
14
e0207836
2019
Homo sapiens (P54802), Homo sapiens
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