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Information on EC 3.1.4.45 - N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase and Organism(s) Homo sapiens and UniProt Accession Q9UK23
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
naglu, phosphodiester alpha-glcnacase, alpha-n-acetylglucosaminyl phosphodiesterase, phosphodiester glycosidase, lysosomal alpha-n-acetylglucosaminidase, n-acetylglucosamine-1-phosphodiester alpha-n-acetylglucosaminidase, alpha-n-acetylglucosaminylphosphodiesterase, n-acetylglucosamine-1-phosphodiester n-acetylglucosaminidase, glcnac-1-phosphodiester alpha-n-acetylglucosaminidase, glcnac-1-phosphodiester-n-acetylglucosaminidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-acetamido-2-deoxy-alpha-D-glucose 1-phosphodiester acetamidodeoxyglucohydrolase
-
-
alpha-N-acetyl-D-glucosamine-1-phosphodiester acetamidodeoxyglucohydrolase
-
-
-
-
alpha-N-acetylglucosaminylphosphodiesterase
-
-
-
-
lysosomal alpha-N-acetyl-glucosaminidase
-
-
-
-
N-acetylglucosamine-1-phosphodiester N-acetylglucosaminidase
-
-
-
-
phosphodiester alpha-GlcNAcase
-
-
-
-
phosphodiester glycosidase
-
-
-
-
UCE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY
75788-84-0
-
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
methyl 6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
-
-
-
?
6-O-(N-acetyl-alpha-D-glucosaminyl)phospho-D-mannose + H2O
N-acetyl-D-glucosamine + D-mannose 6-phosphate
-
-
-
-
?
6-O-(N-acetyl-alpha-D-glucosaminyl)phosphono-D-mannopyranose + H2O
N-acetyl-D-glucosamine + 6-O-phosphono-D-mannopyranose
-
-
-
?
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
N-acetyl-alpha-D-glucosamine 1-phosphate
N-acetyl-D-glucosamine + phosphate
-
-
-
-
?
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
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + H2O
N-acetyl-D-glucosamine + UDP
-
-
-
-
?
glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O
N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose
-
-
-
?
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
-
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
-
catalyzes a crucial step in lysosomal biogenesis, removes a covering N-acetylglucosamine from the mannose 6-phosphate recognition marker on lysosomal hydrolases
-
?
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-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
-
-
-
?
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-alpha-D-glucosaminyl)phospho-alpha-D-mannose + H2O
N-acetyl-D-glucosamine + methyl alpha-D-mannose 6-phosphate
-
low activity
-
-
?
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]-[alpha-L-iduronidase]-L-asparagine + H2O
N-acetyl-D-glucosamine + N-[6-phospho-alpha-D-mannosyl]-[alpha-L-iduronidase]-L-asparagine
-
the enzyme is also active on alpha-L-iduronidase that is recombinantly expressed in transgenic Arabidopsis thaliana seeds
-
-
?
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
-
-
?
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
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
furin
-
UCE is synthesized as an inactive proenzyme that is specifically activated by the endoprotease furin
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
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
-
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
-
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
-
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
-
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
-
mainly localized to the trans-Golgi network and cycles between the network and plasma membrane
-
resides in the trans-Golgi network and cycles between the network and plasma membrane
-
resides primarily in the trans-Golgi network and cycles between the network and the plasma membrane, UCE is endocytosed via clathrin-coated vesicles
-
mutants Y488A/Q492A/E493A/E502stop, Y488A/M494A/N495A/E502stop, Y488A/G496A/E497A/E502stop, Y488A/P498A/L499A/E502stop, Y488A/E493A/E502stop
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
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
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_HUMAN
515
1
56073
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
499fold: recombinant UCE expressed in CHO-K1 cells, 1392fold: recombinant UCE expressed in Sf9 insect cells
-
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
-
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
-
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
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
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
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
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
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
883-886
1986
Homo sapiens
Waheed, A.; Hasilik, A.; von Figura, K.
Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N-acetylglucosaminyl phosphodiesterase
J. Biol. Chem.
256
5717-5721
1981
Homo sapiens
Do, H.; Lee, W.S.; Ghosh, P.; Hollowell, T.; Canfield, W.; Kornfeld, S.
Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin
J. Biol. Chem.
277
29737-29744
2002
Homo sapiens
Lee, W.S.; Rohrer, J.; Kornfeld, R.; Kornfeld, S.
Multiple signals regulate trafficking of the mannose 6-phosphate-uncovering enzyme
J. Biol. Chem.
277
3544-3551
2002
Homo sapiens
Rohrer, J.; Kornfeld, R.
Lysosomal hydrolase mannose 6-phosphate uncovering enzyme resides in the trans-Golgi network
Mol. Biol. Cell
12
1623-1631
2001
Homo sapiens
Wei, Y.; Yen, T.Y.; Cai, J.; Trent, J.O.; Pierce, W.M.; Young, W.W., Jr.
Structural features of the lysosomal hydrolase mannose 6-phosphate uncovering enzyme
Glycoconj. J.
22
13-19
2005
Homo sapiens
Nair, P.; Schaub, B.E.; Huang, K.; Chen, X.; Murphy, R.F.; Griffith, J.M.; Geuze, H.J.; Rohrer, J.
Characterization of the TGN exit signal of the human mannose 6-phosphate uncovering enzyme
J. Cell Sci.
118
2949-2956
2005
Homo sapiens
Chavez, C.A.; Bohnsack, R.N.; Kudo, M.; Gotschall, R.R.; Canfield, W.M.; Dahms, N.M.
Domain 5 of the cation-independent mannose 6-phosphate receptor preferentially binds phosphodiesters (mannose 6-phosphate N-acetylglucosamine ester)
Biochemistry
46
12604-12617
2007
Homo sapiens
Lee, W.S.; Kang, C.; Drayna, D.; Kornfeld, S.
Analysis of mannose 6-phosphate uncovering enzyme mutations associated with persistent stuttering
J. Biol. Chem.
286
39786-39793
2011
Homo sapiens
Das, D.; Lee, W.S.; Grant, J.C.; Chiu, H.J.; Farr, C.L.; Vance, J.; Klock, H.E.; Knuth, M.W.; Miller, M.D.; Elsliger, M.A.; Deacon, A.M.; Godzik, A.; Lesley, S.A.; Kornfeld, S.; Wilson, I.A.
Structure and function of the DUF2233 domain in bacteria and in the human mannose 6-phosphate uncovering enzyme
J. Biol. Chem.
288
16789-16799
2013
Bacteroides ovatus (A7LRK2), Bacteroides ovatus, Bacteroides ovatus ATCC 8483 (A7LRK2), Homo sapiens
He, X.; Pierce, O.; Haselhorst, T.; von Itzstein, M.; Kolarich, D.; Packer, N.H.; Gloster, T.M.; Vocadlo, D.J.; Qian, Y.; Brooks, D.; Kermode, A.R.
Characterization and downstream mannose phosphorylation of human recombinant alpha-L-iduronidase produced in Arabidopsis complex glycan-deficient (cgl) seeds
Plant Biotechnol. J.
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2013
Homo sapiens
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