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Information on EC 3.1.4.45 - N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
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3.1.4.45 N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidaseIUBMB Comments
Acts on a variety of compounds in which N-acetyl-D-glucosamine is alpha-linked to a phosphate group, including the biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the products of EC 2.7.8.17 UDP-N-acetylglucosamine---lysosomal-enzyme N-acetylglucosaminephosphotransferase.
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Word Map
- 3.1.4.45
- mucopolysaccharidosis
-
sanfilippo
- heparan
-
mpsiiib
- hgsnat
-
man-6-p
-
phosphomannosyl
-
n-acetylglucosamine-1-phosphotransferase
- biotechnology
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
naglu, phosphodiester alpha-glcnacase, alpha-n-acetylglucosaminyl phosphodiesterase, phosphodiester glycosidase, lysosomal alpha-n-acetylglucosaminidase, n-acetylglucosamine-1-phosphodiester alpha-n-acetylglucosaminidase, n-acetylglucosamine-1-phosphodiester n-acetylglucosaminidase, glcnac-1-phosphodiester alpha-n-acetylglucosaminidase, alpha-n-acetylglucosaminylphosphodiesterase, glcnac-1-phosphodiester-n-acetylglucosaminidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetamido-2-deoxy-alpha-D-glucose 1-phosphodiester acetamidodeoxyglucohydrolase
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alpha-N-acetyl-D-glucosamine-1-phosphodiester acetamidodeoxyglucohydrolase
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alpha-N-acetylglucosaminylphosphodiesterase
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-
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BACOVA_00430
lysosomal alpha-N-acetyl-glucosaminidase
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lysosomal alpha-N-acetylglucosaminidase
N-acetylglucosamine-1-phosphodiester N-acetylglucosaminidase
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-
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phosphodiester alpha-GlcNAcase
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-
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phosphodiester glycosidase
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-
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UCE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
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-
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SYSTEMATIC NAME
IUBMB Comments
glycoprotein-N-acetyl-D-glucosaminyl-phospho-D-mannose N-acetyl-D-glucosaminylphosphohydrolase
Acts on a variety of compounds in which N-acetyl-D-glucosamine is alpha-linked to a phosphate group, including the biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes and the products of EC 2.7.8.17 UDP-N-acetylglucosamine---lysosomal-enzyme N-acetylglucosaminephosphotransferase.
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CAS REGISTRY NUMBER
COMMENTARY
75788-84-0
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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
2,4-dinitrophenyl alpha-N-acetyl-D-glucosaminide + H2O
2,4-dinitrophenol + alpha-N-acetyl-D-glucosamine
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-
-
-
?
4-nitrophenyl alpha-N-acetyl-D-glucosaminide + H2O
4-nitrophenol + alpha-N-acetyl-D-glucosamine
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-
-
-
?
6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O
N-acetyl-D-glucosamine + 6-phospho-D-mannose
6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O
N-acetyl-D-glucosamine + D-mannose 6-phosphate
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-
-
-
?
6-O-(N-acetyl-alpha-D-glucosaminyl)phosphono-D-mannopyranose + H2O
N-acetyl-D-glucosamine + 6-O-phosphono-D-mannopyranose
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-
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
methyl 6-O-(N-acetyl-D-glucosaminyl)phospho-alpha D-mannose + H2O
N-acetyl-D-glucosamine + methyl 6-phospho-alpha-D-mannopyranoside
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[uteroferrin]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[uteroferrin]-L-asparagine
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-
-
-
?
6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O
N-acetyl-D-glucosamine + 6-phospho-D-mannose
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-
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?
6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O
N-acetyl-D-glucosamine + 6-phospho-D-mannose
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-
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
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-
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal acid hydrolases
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?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
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removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal hydrolases
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?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
catalyzes a crucial step in lysosomal biogenesis, removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal hydrolases
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?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
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-
-
-
?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
-
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
-
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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low activity
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?
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
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-
-
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?
methyl 6-O-(N-acetyl-D-glucosaminyl)phospho-alpha D-mannose + H2O
N-acetyl-D-glucosamine + methyl 6-phospho-alpha-D-mannopyranoside
low activity
-
-
?
methyl 6-O-(N-acetyl-D-glucosaminyl)phospho-alpha D-mannose + H2O
N-acetyl-D-glucosamine + methyl 6-phospho-alpha-D-mannopyranoside
low activity
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-
?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine + phosphate
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-
-
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?
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine + phosphate
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-
-
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?
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine
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-
-
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?
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine
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the enzyme is also active on alpha-L-iduronidase that is recombinantly expressed in transgenic Arabidopsis thaliana seeds
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?
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine + UDP
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?
additional information
?
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catalyzes the second step in the formation of the mannose 6-phosphate recognition marker on lysosomal enzyme oligosaccharides
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?
additional information
?
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removal of the GlcNAc moiety in the trans Golgi network to generate a phosphomonoester, second step of the post-translational modification of lysosomal enzymes with Man-6-P
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?
additional information
?
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D-mannose 6-phosphate phosphodiesters are converted to phosphomonoester
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?
additional information
?
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acts on a variety of compounds with N-acetyl-D-glucosamine alpha-linked to phosphate group, including biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes
-
-
?
additional information
?
-
-
acts on a variety of compounds with N-acetyl-D-glucosamine alpha-linked to phosphate group, including biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes
-
-
?
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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
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine
-
-
-
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal acid hydrolases
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
catalyzes a crucial step in lysosomal biogenesis, removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal hydrolases
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
-
-
-
?
additional information
?
-
-
catalyzes the second step in the formation of the mannose 6-phosphate recognition marker on lysosomal enzyme oligosaccharides
-
?
additional information
?
-
-
removal of the GlcNAc moiety in the trans Golgi network to generate a phosphomonoester, second step of the post-translational modification of lysosomal enzymes with Man-6-P
-
-
?
additional information
?
-
-
D-mannose 6-phosphate phosphodiesters are converted to phosphomonoester
-
-
?
additional information
?
-
-
acts on a variety of compounds with N-acetyl-D-glucosamine alpha-linked to phosphate group, including biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes
-
-
?
additional information
?
-
-
acts on a variety of compounds with N-acetyl-D-glucosamine alpha-linked to phosphate group, including biosynthetic intermediates of the high mannose oligosaccharide components of some lysosomal enzymes
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
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competitive inhibitor
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
furin
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UCE is synthesized as an inactive proenzyme that is specifically activated by the endoprotease furin
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Alzheimer Disease
PLA2G4A/cPLA2-mediated lysosomal membrane damage leads to inhibition of autophagy and neurodegeneration after brain trauma.
Brain Injuries, Traumatic
PLA2G4A/cPLA2-mediated lysosomal membrane damage leads to inhibition of autophagy and neurodegeneration after brain trauma.
Carcinoma, Hepatocellular
Elevated carbohydrate phosphotransferase activity in human hepatoma and phosphorylation of cathepsin D.
Carcinoma, Hepatocellular
[Carbohydrate phosphotransferase in human hepatoma and phosphorylation of cathepsin D]
Genetic Diseases, Inborn
Molecular defects identified by whole exome sequencing in a child with atypical mucopolysaccharidosis IIIB.
Hydrocephalus
Mouse model of Sanfilippo syndrome type B: relation of phenotypic features to background strain.
Infections
Vitamin D3 activates the autolysosomal degradation function against Helicobacter pylori through the PDIA3 receptor in gastric epithelial cells.
Lysosomal Storage Diseases
Clinical and genetic features of 13 patients with mucopolysaccarhidosis type IIIB: Description of two novel NAGLU gene mutations.
Lysosomal Storage Diseases
Deleting the mouse Hsd17b1 gene results in a hypomorphic Naglu allele and a phenotype mimicking a lysosomal storage disease.
Lysosomal Storage Diseases
Generation of two induced pluripotent stem cells lines from a Mucopolysaccharydosis IIIB (MPSIIIB) patient.
Mucolipidoses
Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity.
Mucopolysaccharidoses
A mild form of Mucopolysaccharidosis IIIB diagnosed with targeted next-generation sequencing of linked genomic regions.
Mucopolysaccharidoses
A novel mutation (c.200T>C) in the NAGLU gene of a Korean patient with mucopolysaccharidosis IIIB.
Mucopolysaccharidoses
A Novel Pathogenic Variant in NAGLU (N-Acetyl-Alpha-Glucosaminidase) gene Identified by Targeted Next-Generation Sequencing Followed by in Silico Analysis.
Mucopolysaccharidoses
A rapid and sensitive method for measuring N-acetylglucosaminidase activity in cultured cells.
Mucopolysaccharidoses
An exonic insertion in the NAGLU gene causing Mucopolysaccharidosis IIIB in Schipperke dogs.
Mucopolysaccharidoses
An induced pluripotent stem cell line (TRNDi006-A) from a MPS IIIB patient carrying homozygous mutation of p.Glu153Lys in the NAGLU gene.
Mucopolysaccharidoses
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.
Mucopolysaccharidoses
Cell-Mediated Immunity to NAGLU Transgene Following Intracerebral Gene Therapy in Children With Mucopolysaccharidosis Type IIIB Syndrome.
Mucopolysaccharidoses
Clinical and genetic features of 13 patients with mucopolysaccarhidosis type IIIB: Description of two novel NAGLU gene mutations.
Mucopolysaccharidoses
Coinheritance of novel mutations in NAGLU causing mucopolysaccharidosis type IIIB and in DDHD2 causing spastic paraplegia54 in a Turkish family.
Mucopolysaccharidoses
Disease modeling for Mucopolysaccharidosis type IIIB using patient derived induced pluripotent stem cells.
Mucopolysaccharidoses
Generation of two induced pluripotent stem cells lines from a Mucopolysaccharydosis IIIB (MPSIIIB) patient.
Mucopolysaccharidoses
Induced pluripotent stem cell line (SDQLCHi041-A) from a male patient with mucopolysaccharidosis type IIIB.
Mucopolysaccharidoses
Macrophage enzyme and reduced inflammation drive brain correction of mucopolysaccharidosis IIIB by stem cell gene therapy.
Mucopolysaccharidoses
Molecular basis of mucopolysaccharidosis type IIIB in emu (Dromaius novaehollandiae): an avian model of Sanfilippo syndrome type B.
Mucopolysaccharidoses
Molecular defects identified by whole exome sequencing in a child with atypical mucopolysaccharidosis IIIB.
Mucopolysaccharidoses
Mucopolysaccharidosis IIIB and mild skeletal anomalies: coexistence of NAGLU and CYP26B1 missense variations in the same patient in a Chinese family.
Mucopolysaccharidoses
Mucopolysaccharidosis type IIIB mutations in Chinese patients: Identification of two novel NAGLU mutations and analysis of two cases involving prenatal diagnosis.
Mucopolysaccharidoses
Retrovirally transduced bone marrow has a therapeutic effect on brain in the mouse model of mucopolysaccharidosis IIIB.
Mucopolysaccharidoses
Significant neuropsychiatric symptoms: three mucopolysaccharidosis type IIIB cases, two of whom were siblings with a novel NAGLU gene mutation.
Mucopolysaccharidoses
Trehalose reduces retinal degeneration, neuroinflammation and storage burden caused by a lysosomal hydrolase deficiency.
Mucopolysaccharidoses
Untypically mild phenotype of a patient suffering from Sanfilippo syndrome B with the c.638C>T/c.889C>T (p.Pro213Leu/p.Arg297Ter) mutations in the NAGLU gene.
Mucopolysaccharidosis III
A mild form of Mucopolysaccharidosis IIIB diagnosed with targeted next-generation sequencing of linked genomic regions.
Mucopolysaccharidosis III
A novel mutation in the NAGLU gene associated with Sanfilippo syndrome type B (mucopolysaccharidosis III B).
Mucopolysaccharidosis III
A prospective one-year natural history study of mucopolysaccharidosis types IIIA and IIIB: Implications for clinical trial design.
Mucopolysaccharidosis III
A rapid and sensitive method for measuring N-acetylglucosaminidase activity in cultured cells.
Mucopolysaccharidosis III
Accelerated clinical disease and pathology in mucopolysaccharidosis type IIIB and GalNAc transferase double knockout mice.
Mucopolysaccharidosis III
An exonic insertion in the NAGLU gene causing Mucopolysaccharidosis IIIB in Schipperke dogs.
Mucopolysaccharidosis III
An induced pluripotent stem cell line (TRNDi006-A) from a MPS IIIB patient carrying homozygous mutation of p.Glu153Lys in the NAGLU gene.
Mucopolysaccharidosis III
Assessment of predicted enzymatic activity of ?-N-acetylglucosaminidase variants of unknown significance for CAGI 2016.
Mucopolysaccharidosis III
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.
Mucopolysaccharidosis III
Cell-Mediated Immunity to NAGLU Transgene Following Intracerebral Gene Therapy in Children With Mucopolysaccharidosis Type IIIB Syndrome.
Mucopolysaccharidosis III
Clinical and genetic features of 13 patients with mucopolysaccarhidosis type IIIB: Description of two novel NAGLU gene mutations.
Mucopolysaccharidosis III
Coinheritance of novel mutations in NAGLU causing mucopolysaccharidosis type IIIB and in DDHD2 causing spastic paraplegia54 in a Turkish family.
Mucopolysaccharidosis III
Competitive binding of extracellular accumulated heparan sulfate reduces lysosomal storage defects and triggers neuronal differentiation in a model of Mucopolysaccharidosis IIIB.
Mucopolysaccharidosis III
Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer.
Mucopolysaccharidosis III
Correction of Neurological Disease of Mucopolysaccharidosis IIIB in Adult Mice by rAAV9 Trans-Blood-Brain Barrier Gene Delivery.
Mucopolysaccharidosis III
Differential Uptake of NAGLU-IGF2 and Unmodified NAGLU in Cellular Models of Sanfilippo Syndrome Type B.
Mucopolysaccharidosis III
Disease modeling for Mucopolysaccharidosis type IIIB using patient derived induced pluripotent stem cells.
Mucopolysaccharidosis III
EGFR activation triggers cellular hypertrophy and lysosomal disease in NAGLU-depleted cardiomyoblasts, mimicking the hallmarks of mucopolysaccharidosis IIIB.
Mucopolysaccharidosis III
Generation of two induced pluripotent stem cells lines from a Mucopolysaccharydosis IIIB (MPSIIIB) patient.
Mucopolysaccharidosis III
Identification and characterization of a novel homozygous deletion in the alpha-N-acetylglucosaminidase gene in a patient with Sanfilippo type B syndrome (mucopolysaccharidosis IIIB).
Mucopolysaccharidosis III
Iminosugar C-Glycosides Work as Pharmacological Chaperones of NAGLU, a Glycosidase Involved in MPS IIIB Rare Disease*.
Mucopolysaccharidosis III
Induced pluripotent stem cell line (SDQLCHi041-A) from a male patient with mucopolysaccharidosis type IIIB.
Mucopolysaccharidosis III
Intracranial gene delivery of LV-NAGLU vector corrects neuropathology in murine MPS IIIB.
Mucopolysaccharidosis III
Intravenous administration of human umbilical cord blood cells in an animal model of MPS III B.
Mucopolysaccharidosis III
Molecular analysis of mucopolysaccharidosis type IIIB in Portugal: evidence of a single origin for a common mutation (R234C) in the Iberian Peninsula.
Mucopolysaccharidosis III
Molecular basis of mucopolysaccharidosis type IIIB in emu (Dromaius novaehollandiae): an avian model of Sanfilippo syndrome type B.
Mucopolysaccharidosis III
Mouse model of Sanfilippo syndrome type B: relation of phenotypic features to background strain.
Mucopolysaccharidosis III
Mucopolysaccharidosis IIIB and mild skeletal anomalies: coexistence of NAGLU and CYP26B1 missense variations in the same patient in a Chinese family.
Mucopolysaccharidosis III
Mucopolysaccharidosis type IIIB mutations in Chinese patients: Identification of two novel NAGLU mutations and analysis of two cases involving prenatal diagnosis.
Mucopolysaccharidosis III
Near-Complete Correction of Profound Metabolomic Impairments Corresponding to Functional Benefit in MPS IIIB Mice after IV rAAV9-hNAGLU Gene Delivery.
Mucopolysaccharidosis III
Neurological correction of lysosomal storage in a mucopolysaccharidosis IIIB mouse model by adeno-associated virus-mediated gene delivery.
Mucopolysaccharidosis III
Polymorphic variants (p.Ser141Ser and p.Arg737Gly) at the NAGLU gene are really indicative of pseudodeficiency alleles?
Mucopolysaccharidosis III
Residual N-acetyl-?-glucosaminidase activity in fibroblasts correlates with disease severity in patients with mucopolysaccharidosis type IIIB.
Mucopolysaccharidosis III
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.
Mucopolysaccharidosis III
Retrovirally transduced bone marrow has a therapeutic effect on brain in the mouse model of mucopolysaccharidosis IIIB.
Mucopolysaccharidosis III
Sanfilippo syndrome in Turkey: Identification of novel mutations in subtypes A and B.
Mucopolysaccharidosis III
Sanfilippo type B syndrome: five patients with an R565P homozygous mutation in the alpha-N-acetylglucosaminidase gene from the Okinawa islands in Japan.
Mucopolysaccharidosis III
Significant neuropsychiatric symptoms: three mucopolysaccharidosis type IIIB cases, two of whom were siblings with a novel NAGLU gene mutation.
Mucopolysaccharidosis III
Significantly increased lifespan and improved behavioral performances by rAAV gene delivery in adult mucopolysaccharidosis IIIB mice.
Mucopolysaccharidosis III
Structural and mechanistic insight into the basis of mucopolysaccharidosis IIIB.
Mucopolysaccharidosis III
The alpha-N-acetyl-glucosaminidase gene is transcriptionally activated in male and female gametes prior to fertilization and is essential for seed development in Arabidopsis.
Mucopolysaccharidosis III
Treatment of the mouse model of mucopolysaccharidosis type IIIB with lentiviral-NAGLU vector.
Mucopolysaccharidosis III
Untypically mild phenotype of a patient suffering from Sanfilippo syndrome B with the c.638C>T/c.889C>T (p.Pro213Leu/p.Arg297Ter) mutations in the NAGLU gene.
Muscle Hypotonia
A novel frameshift deletion in NAGLU causing sanfilipo type III-B in an Indian family.
Muscle Spasticity
Coinheritance of novel mutations in NAGLU causing mucopolysaccharidosis type IIIB and in DDHD2 causing spastic paraplegia54 in a Turkish family.
n-acetylglucosamine-1-phosphodiester alpha-n-acetylglucosaminidase deficiency
Disease modeling for Mucopolysaccharidosis type IIIB using patient derived induced pluripotent stem cells.
n-acetylglucosamine-1-phosphodiester alpha-n-acetylglucosaminidase deficiency
Heterozygosity for phosphodiester glycosidase deficiency: a novel human mutation of lysosomal enzyme processing.
n-acetylglucosamine-1-phosphodiester alpha-n-acetylglucosaminidase deficiency
Molecular basis of mucopolysaccharidosis type IIIB in emu (Dromaius novaehollandiae): an avian model of Sanfilippo syndrome type B.
Neoplasms
Elevated carbohydrate phosphotransferase activity in human hepatoma and phosphorylation of cathepsin D.
Neoplasms
Intracerebral gene therapy in children with mucopolysaccharidosis type IIIB syndrome: an uncontrolled phase 1/2 clinical trial.
Neoplasms
Molecular defects identified by whole exome sequencing in a child with atypical mucopolysaccharidosis IIIB.
Neuroblastoma
Competitive binding of extracellular accumulated heparan sulfate reduces lysosomal storage defects and triggers neuronal differentiation in a model of Mucopolysaccharidosis IIIB.
Neurodegenerative Diseases
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.
Neurodegenerative Diseases
Generation of two induced pluripotent stem cells lines from a Mucopolysaccharydosis IIIB (MPSIIIB) patient.
Neurologic Manifestations
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.
Polyneuropathies
Adult-onset painful axonal polyneuropathy caused by a dominant NAGLU mutation.
Stuttering
Analysis of mannose 6-phosphate uncovering enzyme mutations associated with persistent stuttering.
Virus Diseases
Correction of mucopolysaccharidosis type IIIb fibroblasts by lentiviral vector-mediated gene transfer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
4-nitrophenyl alpha-N-acetyl-D-glucosaminide
-
in 0.1 M sodium phosphate, pH 7.3, at 30°C
0.74
dinitrophenyl alpha-N-acetyl-Dglucosaminide
-
in 0.1 M sodium phosphate, pH 7.3, at 30°C
0.04
N-[6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannosyl]-[uteroferrin]-L-asparagine
-
-
0.4
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose
full length enzyme
0.43
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose
delta 102-bp variant
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.062
O-(2-acetamido-2-deoxy-D-glucopyranosylidene)amino-N-phenylcarbamate
-
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
soluble form where transmembrane and cytoplasmic domains were replaced with the HPC4 epitope
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
derived from a lymph node metastasis of a human colon adenocarcinoma, CCL-229, extremely low UCE activity due to a lack of the activating endoprotease furin, addition of furin restores UCE activity
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in tubulovesicular regions of the trans-Golgi network and in clathrin-coated trans Golgi network vesicles and buds, GFP-fusion protein expressed in HeLa cells, localization of mutants E502stop and Y488A/Q492A/E502stop like wild-type
brenda
-
recombinant UCE expressed in CHO-K1 cells and in Sf9 insect cells
-
brenda
-
mainly localized to the trans-Golgi network, cycles between the network and the plasma membrane, type I transmembrane glycoprotein, containing a 24-amino acid signal sequence, a luminal domain of 423 residues, a 27-residue transmembrane region and a 41-residue cytoplasmic tail
brenda
-
resides in the trans-Golgi network and cycles between the network and plasma membrane, type I membrane-spanning glycoprotein with a single 27-residue transmembrane domain and a 41-residue cytoplasmic tail
brenda
-
with a transmembrane segment and a 41-residue cytoplasmic tail, resides primarily in the trans-Golgi network and cycles constitutively between the network and the plasma membrane, regulation of enzyme trafficking by multiple signals, e.g. the 486-YAYHPLQE-493 motif, which is recognized at several sorting sites and facilitates exit from the trans-Golgi network
brenda
-
UCE is a type I homotetrameric transmembrane glycoprotein that is mainly localized to the trans-Golgi network. The signal sequence is excised in the endoplasmic reticulum and upon folding, the catalytically inactive protein is transported to the trans-Golgi network where it is activated by furin cleavage of the prosequence
brenda
-
mainly localized to the trans-Golgi network and cycles between the network and plasma membrane
brenda
-
resides in the trans-Golgi network and cycles between the network and plasma membrane
brenda
-
resides primarily in the trans-Golgi network and cycles between the network and the plasma membrane, UCE is endocytosed via clathrin-coated vesicles
brenda
-
mutants Y488A/Q492A/E493A/E502stop, Y488A/M494A/N495A/E502stop, Y488A/G496A/E497A/E502stop, Y488A/P498A/L499A/E502stop, Y488A/E493A/E502stop
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
-
fibroblasts of individuals with persistent stuttering have decreased enzyme activity, the stuttering phenotype is presumed to arise from neuron dysfunction, overview
metabolism
-
the enzyme is a Golgi enzyme that mediates the second step in the synthesis of the D-mannose 6-phosphate lysosomal targeting signal on acid hydrolases
physiological function
additional information
evolution
the enzyme is a member of the DUF2233-domain protein family. The most conserved residues are Asn130, His217, Arg219, Arg239, Asn268, Asp270, Gly271, Gly272, Gly273, Ser274, Arg303, and Val305. These residues are clustered on one side of the protein, and almost all have significant surface exposure. Of these, Asn268, Asp270, Gly271-273, and Ser274 are part of the highly conserved A(I/L)NLDGGGS(T/S/A)T motif present throughout the DUF2233 family and located in helix H7 and in the preceding loop between beta17 and H7 near the center of the conserved site
evolution
-
the enzyme is a member of the DUF2233-domain protein family. The most conserved residues are Asn130, His217, Arg219, Arg239, Asn268, Asp270, Gly271, Gly272, Gly273, Ser274, Arg303, and Val305. These residues are clustered on one side of the protein, and almost all have significant surface exposure. Of these, Asn268, Asp270, Gly271-273, and Ser274 are part of the highly conserved A(I/L)NLDGGGS(T/S/A)T motif present throughout the DUF2233 family and located in helix H7 and in the preceding loop between beta17 and H7 near the center of the conserved site
-
physiological function
-
most lysosomal enzymes including alpha-L-iduronidase require a mannose 6-phosphate tag for efficient uptake and lysosomal delivery in human cells. In mammalian cells, the mannose 6-phosphate tag is generated by the sequential action of two enzymes: UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, also known as GlcNAc-1-phosphotransferase, and N-acetylglucosamine 1-phosphodiester alpha-N-acetylglucosaminidase, i.e. the uncovering enzyme
physiological function
-
the enzyme is is involved in targeting of lysosomal enzymes
additional information
a sulfate ion is bound near Gly272-Gly273 of the GGGS sequence and anchored by conserved residues Arg239 and Arg303 and may represent the binding site for the phosphate moiety of the substrate. Asn130, Asp270, and Ser274 are potential catalytic residues
additional information
-
a sulfate ion is bound near Gly272-Gly273 of the GGGS sequence and anchored by conserved residues Arg239 and Arg303 and may represent the binding site for the phosphate moiety of the substrate. Asn130, Asp270, and Ser274 are potential catalytic residues
additional information
-
the crystal structure of the BACOVA_00430 protein from Bacteroides ovatus is used to model the luminal portion of human enzyme. The Cys51-Cys221 disulfide bond is not absolutely essential for folding or enzyme activity
additional information
-
a sulfate ion is bound near Gly272-Gly273 of the GGGS sequence and anchored by conserved residues Arg239 and Arg303 and may represent the binding site for the phosphate moiety of the substrate. Asn130, Asp270, and Ser274 are potential catalytic residues
-
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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). NAGPA_BOVIN
527
1
57223
Swiss-Prot
Secretory Pathway (Reliability: 1)
NAGPA_HUMAN
515
1
56073
Swiss-Prot
Secretory Pathway (Reliability: 1)
NAGPA_MOUSE
517
2
56044
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A8B6CVZ6_MYTGA
328
1
36791
TrEMBL
other Location (Reliability: 1)
G0QYD5_ICHMG
Ichthyophthirius multifiliis (strain G5)
570
0
65019
TrEMBL
other Location (Reliability: 3)
A0A8M1NEE2_DANRE
586
1
64086
TrEMBL
Secretory Pathway (Reliability: 1)
G0QM08_ICHMG
Ichthyophthirius multifiliis (strain G5)
236
0
26888
TrEMBL
other Location (Reliability: 3)
G0QSY5_ICHMG
Ichthyophthirius multifiliis (strain G5)
379
0
42643
TrEMBL
other Location (Reliability: 1)
B7PKH8_IXOSC
2582
1
287020
TrEMBL
other Location (Reliability: 1)
A0A8B6BJR5_MYTGA
292
1
31942
TrEMBL
other Location (Reliability: 4)
A0A6J8AYY6_MYTCO
597
2
65603
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8B6EVH2_MYTGA
388
0
43929
TrEMBL
other Location (Reliability: 1)
G0R6K0_ICHMG
Ichthyophthirius multifiliis (strain G5)
414
0
47025
TrEMBL
other Location (Reliability: 2)
G0QQ11_ICHMG
Ichthyophthirius multifiliis (strain G5)
418
0
47929
TrEMBL
other Location (Reliability: 1)
B7QHE0_IXOSC
2084
0
231854
TrEMBL
other Location (Reliability: 2)
A0A8B6CX20_MYTGA
427
1
47853
TrEMBL
other Location (Reliability: 4)
E0W4D6_PEDHC
2523
1
282397
TrEMBL
Mitochondrion (Reliability: 4)
G0QX88_ICHMG
Ichthyophthirius multifiliis (strain G5)
381
0
43507
TrEMBL
other Location (Reliability: 1)
G0R6J8_ICHMG
Ichthyophthirius multifiliis (strain G5)
519
0
59388
TrEMBL
Secretory Pathway (Reliability: 1)
G0QL29_ICHMG
Ichthyophthirius multifiliis (strain G5)
838
0
96299
TrEMBL
other Location (Reliability: 2)
G0R0P2_ICHMG
Ichthyophthirius multifiliis (strain G5)
459
0
51131
TrEMBL
other Location (Reliability: 3)
G0QQ49_ICHMG
Ichthyophthirius multifiliis (strain G5)
862
0
97732
TrEMBL
other Location (Reliability: 4)
G0QYL0_ICHMG
Ichthyophthirius multifiliis (strain G5)
535
1
61331
TrEMBL
Secretory Pathway (Reliability: 1)
B7PYB2_IXOSC
667
0
71619
TrEMBL
Mitochondrion (Reliability: 4)
A0A8B6G9K0_MYTGA
311
0
34653
TrEMBL
Secretory Pathway (Reliability: 4)
D7GDC5_PROFC
Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1)
315
0
33166
TrEMBL
-
G0R0E3_ICHMG
Ichthyophthirius multifiliis (strain G5)
787
0
85197
TrEMBL
other Location (Reliability: 2)
A0A6J8DFJ1_MYTCO
271
0
30223
TrEMBL
other Location (Reliability: 1)
A0A0A8PEZ7_9ACTN
315
0
33190
TrEMBL
-
A0A8B6G9K2_MYTGA
315
1
35234
TrEMBL
Secretory Pathway (Reliability: 1)
G0QQX2_ICHMG
Ichthyophthirius multifiliis (strain G5)
502
0
58122
TrEMBL
other Location (Reliability: 1)
G0QQP9_ICHMG
Ichthyophthirius multifiliis (strain G5)
726
0
83733
TrEMBL
other Location (Reliability: 2)
A0A812C156_SEPPH
1021
3
114051
TrEMBL
Secretory Pathway (Reliability: 2)
G0R6L7_ICHMG
Ichthyophthirius multifiliis (strain G5)
520
0
58848
TrEMBL
Secretory Pathway (Reliability: 1)
G0QSR2_ICHMG
Ichthyophthirius multifiliis (strain G5)
3573
4
405962
TrEMBL
Secretory Pathway (Reliability: 1)
A7LRK2_BACO1
Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
315
0
34351
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
129000
69000
additional information
additional information
-
1885 Da, peptides of amino acid position 80 to 84 and 268 to 274, determined by LC/ESI-MS/MS analysis, soluble form
additional information
-
2797 Da, peptide of amino acid position 159 to 183, determined by MALDI-TOF and by LC/MS, soluble form
additional information
-
2878 Da, peptide of amino acid position 331 to 355, determined by LC/MS, soluble form
additional information
-
2925 Da, peptide of amino acid position 305 to 355, determined by MALDI-TOF and by LC/MS, soluble form
additional information
-
3124 Da, peptides of amino acid position 54 to 69 and 94 to 108, determined by LC/ESI-MS/MS analysis, soluble form
additional information
-
3230 Da, peptides of amino acid position 1 to 4 and 159 to 182, determined by LC/ESI-MS/MS analysis, soluble form
additional information
-
4023 Da, peptide of amino acid position 228 to 264, determined by MALDI-TOF and by LC/MS, soluble form
additional information
-
4337 Da, peptides of amino acid position 228 to 264 and 265 to 267, determined by LC/ESI-MS/MS analysis, soluble form
additional information
-
880 Da, peptide of amino acid position 369 to 376, determined by MALDI-TOF, soluble form
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
glycoprotein contains asparagine-linked oligosaccharides and sialic acid
glycoprotein
-
UCE is core glycosylated as it enters the endoplasmic reticulum, traverses the Golgi apparatus where the oligosaccahide is processed to a complex-type structure
glycoprotein
-
N-linked glycosylation of Asn159, Asn165, Asn247 and Asn317 determined by PNGase F treatment and MS analysis, soluble form
proteolytic modification
-
UCE is synthesized as an inactive proenzyme that is activated by the endoprotease furin, which is localized in the trans-Golgi network and cleaves an RARLPR/D sequence to release a 24-amino acid propiece
proteolytic modification
-
the human uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin in the trans-Golgi network
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged wild-type and selenomethionine-labeled enzyme, sitting nanodroplet vapor diffusion method, mixing of 200 nl of 21 mg/ml protein in 20 mM HEPES, pH 8.0, 200 mM NaCl, 40 mM imidazole, and 1 mM TCEP, with 200 nl of reservoir solution containing 0.2 M Li2SO4, 30% PEG 4000, and 0.1 M Tris, pH 8.5, and equilibration against 0.05 ml of reservoir solution, 4°C, 10% v/v ethylene glycol as a cryoprotectant, X-ray diffraction structure determination and analysis at 1.80 A resolution, modeling, the crystal structure of the BACOVA_00430 protein from Bacteroides ovatus is used to model the luminal portion of the human enzyme N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
hanging drop vapour diffusion method, in 2.0 M (NH4)2SO4 with 3% (v/v) glycerol
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C115X
-
site-directed mutagenesis, the mutation greatly impairs folding of the enzyme, the mutant is retained in the endoplasmic reticulum
C132X
-
site-directed mutagenesis, the mutation greatly impairs folding of the enzyme, the mutant is retained in the endoplasmic reticulum
C221L
-
site-directed mutagenesis, the mutation leads to loss of enzymatic activity
C51M/C221L
-
site-directed mutagenesis, the mutant folds adequately and is trafficked to the Golgi where it is cleaved by furin, the mutant shows only 9.7% of wild-type activity
E502stop
-
similar localization to the trans Golgi network as the wild-type, lumenal domain of UCE was replaced with monomeric GFP
F513S
-
naturally occuring Phe513SerfsX113 frameshift mutation that adds 113 amino acids to the C-terminus of the cytoplasmic tail of the protein including a VWLL sequence, causing rapid degradation via the proteasomal system
H510stop
H84Q
-
naturally occuring mutation that impairs folding and in addition, decreases the specific activity of the enzyme, to about half the relative specific activity of wild-type enzyme, but folds sufficiently to traffic to the Golgi
N281A
-
site-directed mutagenesis, the mutant is recombinantly expressed but retained in the endoplasmic reticulum
Q225H
-
site-directed mutagenesis, exchange of the human residue for the residue of protein BACOVA_00430 from Bacteroides ovatus, the mutant shows 5.8% of wild-type activity
R328C
-
naturally occuring mutation that impairs folding in the endoplasmic reticulum, resulting in degradation of a significant portion by the proteasomal system. The mutation leads to lower cellular UCE activity, and might be involved in persistent stuttering phenomena. The R328C mutant forms oligomers with the wild-type enzyme
T227R
-
site-directed mutagenesis, exchange of the human residue for the residue of protein BACOVA_00430 from Bacteroides ovatus, the mutant shows 0.1% of wild-type activity
V318A
-
site-directed mutagenesis, the mutant is recombinantly expressed but retained in the endoplasmic reticulum
Y486A
-
mutated residue is required for efficient return of the enzyme from endosomes to the trans-Golgi network, mutant UCE is internalized normally but accumulates on the cell surface, 26-36% of activity on the cell surface compared with 1-3% of wild-type activity, because of increased recycling to the plasma membrane, kinetics of internalization
Y486stop
-
mutant with 16% of total enzyme activity on the cell surface at steady state compared with 1-3% of wild-type activity, kinetics of internalization
Y488A
Y488A/E493A/E502stop
-
localized to a large extent to the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/E502stop
-
localized to a large extent to the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/G496A/E497A/E502stop
-
localized to a large extent to the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/M494A/E502stop
-
localization shows endosome pattern, not at the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/M494A/N495A/E502stop
-
intermediate phenotype, localized to the cell surface and to the trans Golgi network, lumenal domain of UCE was replaced with monomeric GFP
Y488A/N495A/E502stop
-
localization shows endosome pattern, not at the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/P498A/L499A/E502stop
-
localized to a large extent to the cell surface, lumenal domain of UCE was replaced with monomeric GFP
Y488A/Q492A/E493A/E502stop
-
intermediate phenotype, localized to the cell surface and to the trans Golgi network, lumenal domain of UCE was replaced with monomeric GFP
Y488A/Q492A/E493A/M494A/N495A/E502stop
-
localization shows endosome pattern and localized to the Golgi, lumenal domain of UCE was replaced with monomeric GFP
Y488A/Q492A/E502stop
-
similar localization to the trans Golgi network as the wild-type, lumenal domain of UCE was replaced with monomeric GFP
additional information
H510stop
-
mutant with 7% of total enzyme activity on the cell surface at steady state compared with 1-3% of wild-type activity, kinetics of internalization
Y488A
-
mutant of the cytosolic tail disrupting the tyrosine-based endocytosis motif
Y488A
-
mutant with 63% of total enzyme activity on the cell surface at steady state compared with 1-3% of wild-type activity, kinetics of internalization
Y488A
-
mutation in the 488YHPL internalization signal present in the cytoplasmic tail, mutant UCE accumulates on the cell surface
additional information
-
soluble form lacking residues 1-49, transmembrane and cytoplasmic domains are replaced by the HPC4 epitope
additional information
-
generation of the enzyme in soluble form for conducting the in vitro phosphorylation of purified recombinant lysosomal enzymes
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
499fold: recombinant UCE expressed in CHO-K1 cells, 1392fold: recombinant UCE expressed in Sf9 insect cells
-
recombinant enzyme with TEV cleavage site and His6-tag by nickel affinity chromatography, tag cleavage by tobacco etch virus protease, another step of nickel affinity chromatography, and centrifugal ultrafiltration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in mouse L-cells, expression of UCE containing green fluorescent protein in place of the luminal domain in HeLa cells
-
polymerase incomplete primer extension cloning method, recombinant expression of enzyme with TEV cleavage site and His6-tag in Escherichia coli as wild-type and selenomethionine-labeled enzyme
two splice forms, one of these isoforms lacks 102-base pairs corresponding to exon 8 of the 10 exons present in the genomic DNA and is predominantly expressed in brain. Expression of wild-type and mutant enzymes in HeLa cells
-
wild-type and mutant UCE expression in mouse L-cells, expression of various green fluorescent protein-UCE fusion proteins in HeLa cells
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
the uncovering enzyme is generated as soluble enzyme and so can be used to conduct the in vitro phosphorylation of purified recombinant lysosomal enzymes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kornfeld, R.; Bao, M.; Brewer, K.; Noll, C.; Canfield, W.
Molecular cloning and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
J. Biol. Chem.
274
32778-32785
1999
Homo sapiens (Q9UK23), Homo sapiens
brenda
Kornfeld, R.; Bao, M.; Brewer, K.; Noll, C.; Canfield, W.
Purification and multimeric structure of bovine N-acetylglucosamine-phosphodiester alpha-N-acetylglucosaminidase
J. Biol. Chem.
273
23203-23210
1998
Bos taurus
brenda
Page, T.; Zhao, K.W.; Tao, l.; Miller, A.L.
Purification and characterization of human lymphoblast N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
Glycobiology
6
619-626
1996
Homo sapiens
brenda
Lee, J.K.; Pierce, M.
Purification and characterization of human serum N-acetylgluosamine-1-phosphodiester alpha-N-acetylglucosaminidase
Arch. Biochem. Biophys.
319
413-425
1995
Cricetulus griseus, Homo sapiens
brenda
Gheesling Mullis, K.; Huynh, M.; Kornfeld, R.H.
Purification and kinetic parameters of bovine liver N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
J. Biol. Chem.
269
1718-1726
1994
Bos taurus, Homo sapiens
brenda
Gheesling Mullis, K.; Kornfeld, R.H.
Characterization and immunolocalisation of bovine N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
J. Biol. Chem.
269
1727-1733
1994
Bos taurus, Mus musculus
brenda
Ben-Yoseph, Y.; Potier, M.; Pack, B.A.; Mitchell, D.A.; Melancon, S.B.; Nadler, H.L.
Molecular size of N-acetylglucosaminylphosphotransferase and alpha-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation
Biochem. J.
235
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