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Information on EC 3.2.1.50 - alpha-N-acetylglucosaminidase
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EC Tree
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 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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetamido-2-deoxy-alpha-D-glucoside acetamidodeoxyglucohydrolase
AgnC
alpha-acetylglucosaminidase
alpha-N-acetylglucosaminidase
BMN 250
tralesinidase alfa, a fusion protein of lysosomal alpha-N-acetylglucosaminidase with insulin-like growth factor 2
N-acetyl-alpha-glucosaminidase
NAG
NAGase
NAGLU
NAG
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(GlcNAcalpha(1-4))n + H2O = (GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of N-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
alpha-N-acetyl-D-glucosaminide N-acetylglucosaminohydrolase
Hydrolyses UDP-N-acetylglucosamine.
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CAS REGISTRY NUMBER
COMMENTARY
37288-40-7
-
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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
(GlcNAcalpha(1-4))n + H2O
(GlcNAcalpha(1-4))n-1 + 2-(acetylamino)-2-deoxy-beta-D-glucopyranose
2,4-dinitrophenyl-alpha-N-acetyl-D-glucosaminide + H2O
2,4-dinitrophenol + N-acetyl-D-glucosamine
25°C
-
-
?
2-nitrophenyl alpha-N-acetylglucosaminide + H2O
2-nitrophenol + alpha-N-acetylglucosamine
-
-
-
-
?
4-methylumbelliferyl 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O
?
-
-
-
?
4-methylumbelliferyl 4-O-N-acetyl-alpha-D-glucosaminyl-beta-D-galactoside + H2O
N-acetyl-alpha-D-glucosamine + 4-methylumbelliferyl beta-D-galactosaminide
-
-
-
-
?
4-methylumbelliferyl 6-O-N-acetyl-alpha-D-glucosaminyl-beta-D-galactoside + H2O
N-acetyl-alpha-D-glucosamine + 4-methylumbelliferyl beta-D-galactosaminide
-
slow reaction
-
-
?
4-methylumbelliferyl N-acetyl-alpha-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-alpha-D-glucosamine
4-methylumbelliferyl-2-acetamide-2-deoxy-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + 2-acetamide-2-deoxy-alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl N-acetyl-alpha-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-alpha-D-glucosamine
-
slow reaction
-
-
?
4-nitrophenyl-alpha-N-acetyl-D-glucosaminide + H2O
4-nitrophenol + N-acetyl-alpha-D-glucose
25°C
-
-
?
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
N-acetyl-alpha-D-glucosamine + 4-nitrophenol
methylumbelliferyl-N-acetyl-alpha-D-glucosaminide + H2O
methylumbelliferone + N-acetyl-alpha-D-glucosamine
methylumbelliferyl-N-acetylglucosamine + H2O
methylumbelliferone + N-acetylglucosamine
-
-
-
?
methylumbelliferyl-N-acetylglucosamine-6-sulfate + H2O
methylumbelliferone + N-acetylglucosamine-6-sulfate
-
-
-
?
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal + H2O
N-acetyl-alpha-D-glucosamine + 1-methoxyphenyl-Gal
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
(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
-
-
-
?
(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
-
-
?
(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
-
-
-
?
4-methylumbelliferyl N-acetyl-alpha-D-glucosaminide + H2O
4-methylumbelliferone + N-acetyl-alpha-D-glucosamine
-
efficient substrate
-
-
?
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
-
-
-
-
?
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
N-acetyl-alpha-D-glucosamine + 4-nitrophenol
-
-
-
?
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide + H2O
N-acetyl-alpha-D-glucosamine + 4-nitrophenol
-
-
-
?
cell surface mucin + H2O
N-acetyl-alpha-D-glucosamine + ?
-
-
-
?
cell surface mucin + H2O
N-acetyl-alpha-D-glucosamine + ?
-
-
-
?
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
-
-
-
?
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal + H2O
N-acetyl-alpha-D-glucosamine + 1-methoxyphenyl-Gal
-
-
-
?
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal + H2O
N-acetyl-alpha-D-glucosamine + 1-methoxyphenyl-Gal
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
porcine gastric mucin + H2O
N-acetyl-alpha-D-glucosamine + ?
-
the enzyme specifically hydrolyzes alpha-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin
-
-
?
porcine gastric mucin + H2O
N-acetyl-alpha-D-glucosamine + ?
-
-
-
?
porcine gastric mucin + H2O
N-acetyl-alpha-D-glucosamine + ?
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + H2O
uridine-5'-diphosphate + 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
-
-
-
?
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
?
-
-
no activity with 4-nitrophenyl N-acetyl-beta-D-glucosaminide, 4-nitrophenyl N-acetyl-alpha-D-galactosaminide, 4-nitrophenyl N-acetyl-beta-D-galactosaminide, 4-nitrophenyl alpha-D-glucosaminide, 4-nitrophenyl beta-D-glucosaminide, 4-nitrophenyl alpha-D-galactosaminide, 4-nitrophenyl beta-D-galactosaminide, 4-nitrophenyl alpha-D-fucosaminide, 4-nitrophenyl beta-D-fucosaminide, 4-nitrophenyl alpha-D-mannosaminide, 4-nitrophenyl beta-D-mannosaminide, 4-nitrophenyl alpha-D-xylosaminide, and 4-nitrophenyl beta-D-xylosaminide. Alpha1,2- and alpha1,3-linked N-acetyl-alpha-D-glucosaminides are resistant to this enzyme
-
-
?
additional information
?
-
-
swollen chitin and oligosaccharide above (GlcNAc)4 are not hydrolyzed by the enzyme
-
?
additional information
?
-
no activity against any of the GlcNAc1,2-(1-methoxyphenyl)Gal, GlcNAc-1,3-(1-methoxyphenyl)Gal, GlcNAc-1,6-(1-methoxyphenyl)Gal, andGlcNAc-1,4-(1-methoxyphenyl)Glc substrates
-
-
?
additional information
?
-
-
no activity against any of the GlcNAc1,2-(1-methoxyphenyl)Gal, GlcNAc-1,3-(1-methoxyphenyl)Gal, GlcNAc-1,6-(1-methoxyphenyl)Gal, andGlcNAc-1,4-(1-methoxyphenyl)Glc substrates
-
-
?
additional information
?
-
no activity against any of the GlcNAc1,2-(1-methoxyphenyl)Gal, GlcNAc-1,3-(1-methoxyphenyl)Gal, GlcNAc-1,6-(1-methoxyphenyl)Gal, andGlcNAc-1,4-(1-methoxyphenyl)Glc substrates
-
-
?
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
-
-
?
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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
UDP-N-acetyl-alpha-D-glucosamine + H2O
uridine-5'-diphosphate + 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
-
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
-
-
-
?
(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
-
-
?
(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
-
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Hg2+
additional information
-
Ca2+, Mg2+, Zn2+, Mn2+, Ni2+, and Co2+, do not affect enzyme activity at 5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
colombin
-
active component of antivenom preparation from Aristolodia albida, competitive
-
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
-
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
-
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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%
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.74
2,4-dinitrophenyl-alpha-N-acetyl-D-glucosaminide
pH 7.3
0.043 - 0.61
2-nitrophenyl alpha-N-acetylglucosaminide
-
form I 0.067, form II 0.043
-
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
0.39
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
4.3
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
wild-type, pH 7.4, 37°C
7.8
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
C-terminal deletion mutant, pH 7.4, 37°C
0.2
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
wild-type, pH 7.4, 37°C
0.28
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
C-terminal deletion mutant, pH 7.4, 37°C
0.043 - 0.61
o-nitrophenyl-alpha-N-acetylglucosaminide
-
0.23-0.25 in the presence of 0.025% 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.5
2,4-dinitrophenyl-alpha-N-acetyl-D-glucosaminide
pH 7.3
0.26
4-nitrophenyl N-acetyl-alpha-D-glucosaminopyranoside
pH 7.3
0.69
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
wild-type, pH 7.4, 37°C
0.74
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
C-terminal deletion mutant, pH 7.4, 37°C
1.24
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
wild-type, pH 7.4, 37°C
6.19
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
C-terminal deletion mutant, pH 7.4, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
C-terminal deletion mutant, pH 7.4, 37°C
0.16
4-nitrophenyl-N-acetyl-alpha-D-glucosaminide
wild-type, pH 7.4, 37°C
6.2
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
wild-type, pH 7.4, 37°C
22.1
N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal
C-terminal deletion mutant, pH 7.4, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0062
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
0.1
0.115 - 1.2
-
purified enzyme, p-nitrophenyl-N-acetyl-alpha-D-glucosaminide as substrate
0.2
wild-type, substrate N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal, pH 7.4, 37°C
0.58
-
purified enzyme, methylumbelliferyl-N-acetyl-alpha-D-glucosaminide as substrate
2.82
C-terminal deletion mutant, substrate N-acetyl-alpha-D-Gluc-1,4-(1-methoxyphenyl)Gal, pH 7.4, 37°C
additional information
0.1
C-terminal deletion mutant, substrate 4-nitrophenyl-N-acetyl-alpha-D-glucosaminide, pH 7.4, 37°C
0.1
wild-type, substrate 4-nitrophenyl-N-acetyl-alpha-D-glucosaminide, pH 7.4, 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.4
4.5
4.6
4.7
4.8
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
no acitvity in Phlebotomus papatasi
desert and oasis flies studied, male and female, Neot Hakikar (oasis), Jordan Valley spring (wet), Kfar Adumim starved (arid), Jordan Valley autumn (arid)
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
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
physiological function
enzyme acts as specific glycosidase required for degrading alpha-GlcNAc-capped O-glycans of the class III mucin secreted from the stomach and duodenum. The agnC gene-disrupted strain shows significantly reduced growth on the class III mucin-containing medium compared with the wild type strain
physiological function
-
the enzyme is important for assimilation of gastroduodenal mucin by Bacillus bifidum and also applicable to production of prebiotic oligosaccharides from porcine gastric mucin
physiological function
-
enzyme acts as specific glycosidase required for degrading alpha-GlcNAc-capped O-glycans of the class III mucin secreted from the stomach and duodenum. The agnC gene-disrupted strain shows significantly reduced growth on the class III mucin-containing medium compared with the wild type strain
-
Show AA Sequence and Transmembrane Helices (220 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
x * 220000, wild-type, x * 120000, C-terminal deletion mutant, SDS-PAGE
220000
x * 220000, wild-type, x * 120000, C-terminal deletion mutant, SDS-PAGE
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
x * 220000, wild-type, x * 120000, C-terminal deletion mutant, SDS-PAGE
?
-
x * 220000, wild-type, x * 120000, C-terminal deletion mutant, SDS-PAGE
-
?
-
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
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
glycoprotein
the enzyme has 6 putative N-glycosylation sites at N261, N272, N435, N503, N526 and N532
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E601A
mutation in the active site, lack of enzymatic activity
mutagenesis of Glu-483
mutation in the active site, less enzymatic activity
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
deletion of the C-terminal region containing several carbohydrate-binding module 32 domains significantly reduces the activity for porcine gastric mucin,while activity against GlcNAc1,4-(1-methoxyphenyl)Gal is markedly enhanced. A deletion construct containing the C-terminal carbohydrate-binding module-C2 to carbohydrate-binding module-C6 domains binds strongly to porcine gastric mucin
additional information
-
deletion of the C-terminal region containing several carbohydrate-binding module 32 domains significantly reduces the activity for porcine gastric mucin,while activity against GlcNAc1,4-(1-methoxyphenyl)Gal is markedly enhanced. A deletion construct containing the C-terminal carbohydrate-binding module-C2 to carbohydrate-binding module-C6 domains binds strongly to porcine gastric mucin
additional information
-
deletion of the C-terminal region containing several carbohydrate-binding module 32 domains significantly reduces the activity for porcine gastric mucin,while activity against GlcNAc1,4-(1-methoxyphenyl)Gal is markedly enhanced. A deletion construct containing the C-terminal carbohydrate-binding module-C2 to carbohydrate-binding module-C6 domains binds strongly to porcine gastric mucin
-
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
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
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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
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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
-
in citrate buffer, pH 6.0, no inactivation by 50°C heating, 90% inactivation at 70°C for 30 min
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
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
entire inactivation by gel electrophoresis in the presence of sodium dodecylsulfate
-
no proteolysis with pronase, bromelain and trypsin, 15% loss of activity after 30 min incubation with papain
-
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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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.9% NaCl, cultivated cells centrifuged at 1500 * g, 2 weeks, no loss of activity
-
37°C, 4 days, no loss of activity, but complete dissociation of form I into form II
-
4°C, 10 mM sodium phosphate buffer, pH 7.2, 150 mM NaCl, 1 year, no significant loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
butyl-Sepharose 4 column chromatography and Q-Sepharose column chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination of Sanfilippo type B syndrome patients
-
expression in Escherichia coli
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
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Werries, E.; Wollek, E.; Gottschalk, A.; Buddecke, E.
Separation of N-acetyl-alpha-glucosaminidase and N-acetyl-alpha-galactosaminidase from ox spleen. Cleavage of the O-glycosidic linkage between carbohydrate and polypeptide in ovine and bovine submaxillary glycoprotein by N-acetyl-alpha-galactosaminidase
Eur. J. Biochem.
10
445-449
1969
Bos taurus
brenda
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
-
brenda
Hook, G.E.R.; Gilmore, L.B.
Hydrolases of pulmonary lysosomes and lamellar bodies
J. Biol. Chem.
257
9211-9220
1982
Oryctolagus cuniculus
brenda
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
brenda
von Figura, K.
Human alpha-N-acetylglucosaminidase. 1. Purification and properties
Eur. J. Biochem.
80
525-533
1977
Homo sapiens
-
brenda
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
brenda
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
brenda
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
brenda
Mersman, G.; von Figura, K.; Buddecke, E.
Physical properties and biological activities of two forms of alpha-N-acetylglucosaminidase from bovine spleen
Biochim. Biophys. Acta
364
88-96
1974
Bos taurus
brenda
Bannister, J.V.; Phizackerley, P.J.R.
Purification of an N-acetylglucosaminidase from the limpet Patella vulgata L.
FEBS Lett.
29
313-317
1973
Patella vulgata
brenda
Weissmann, B.; Rowin, G.; Marshall, J.; Friederici, D.
Mammalian alpha-acetylglucosaminidase. Enzymic properties, tissue distribution, and intracellular localization
Biochemistry
6
207-214
1967
Rattus norvegicus, Sus scrofa
brenda
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
brenda
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
-
brenda
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
brenda
Oliveira, F.W.; Chavante, S.F.; Santos, E.A.; Dietrich, C.P.; Nader, H.B.
Appearance and fate of a beta-galactanase, alpha,beta-galactosidases, heparan sulfate and chondroitin sulfate degrading enzymes during embryonic development of the mollusc Pomacea sp.
Biochim. Biophys. Acta
1200
241-246
1994
Pomacea sp.
brenda
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
brenda
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
brenda
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
brenda
Nok, A.J.; Shuaibu, M.N.; Choudhry, M.K.; Oyebanjo, O.; Ibrahim, S.; Williams, S.
N-Acetyl alpha-D-glucosaminidase from the venom of African puff adder (Bitis arietans)
J. Biochem. Mol. Toxicol.
15
221-227
2001
Bitis arietans
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Jacobson, R.L.; Studentsky, L.; Schlein, Y.
Glycolytic and chitinolytic activities of Phlebotomus papatasi (Diptera: Psychodidae) from diverse ecological habitats
Folia Parasitol.
54
301-309
2007
no acitvity in Phlebotomus papatasi
brenda
Ryazantsev, S.; Yu, W.H.; Zhao, H.Z.; Neufeld, E.F.; Ohmi, K.
Lysosomal accumulation of SCMAS (subunit c of mitochondrial ATP synthase) in neurons of the mouse model of mucopolysaccharidosis III B
Mol. Genet. Metab.
90
393-401
2007
Mus musculus
brenda
Ficko-Blean, E.; Stubbs, K.A.; Nemirovsky, O.; Vocadlo, D.J.; Boraston, A.B.
Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB
Proc. Natl. Acad. Sci. USA
105
6560-6565
2008
Clostridium perfringens (A0A0H2YU91)
brenda
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
brenda
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
brenda
Fujita, M.; Tsuchida, A.; Hirata, A.; Kobayashi, N.; Goto, K.; Osumi, K.; Hirose, Y.; Nakayama, J.; Yamanoi, T.; Ashida, H.; Mizuno, M.
Glycoside hydrolase family 89 alpha-N-acetylglucosaminidase from Clostridium perfringens specifically acts on GlcNAc alpha1,4Gal beta1R at the non-reducing terminus of O-glycans in gastric mucin
J. Biol. Chem.
286
6479-6489
2011
Clostridium perfringens (Q8XM24), Clostridium perfringens, Clostridium perfringens 13 (Q8XM24)
brenda
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
brenda
Shimada, Y.; Watanabe, Y.; Wakinaka, T.; Funeno, Y.; Kubota, M.; Chaiwangsri, T.; Kurihara, S.; Yamamoto, K.; Katayama, T.; Ashida, H.
alpha-N-acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes alpha-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin
Appl. Microbiol. Biotechnol.
99
3941-3948
2015
Bifidobacterium bifidum
brenda
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
brenda
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
brenda
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Release 2023.1 (January 2023)
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