Information on EC 2.7.8.17 - UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.17
-
RECOMMENDED NAME
GeneOntology No.
UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:lysosomal-enzyme N-acetylglucosaminephosphotransferase
Some other glycoproteins with high-mannose can act as acceptors, but much more slowly than lysosomal enzymes.
CAS REGISTRY NUMBER
COMMENTARY hide
84012-69-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
ARG-17 strain
-
-
Manually annotated by BRENDA team
ARG-17 strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + alpha-L-fucosidase
UMP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-methyl D-mannoside
UMP + 6-(N-acetyl-D-glucosaminyl-phospho)-alpha-methyl D-mannoside
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-methyl-D-mannoside
UMP + 6-(N-acetyl-D-glucosaminyl-phospho)-alpha-methyl D-mannoside
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-N-acetylglucosaminidase
UMP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-hexosaminidase
UMP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + cathepsin A
UMP + ?
show the reaction diagram
-
capthepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + DNase I
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-cathepsin Z D-mannose
UMP + lysosomal-cathepsin Z N-acetyl-D-glucosaminyl-phospho-D-mannose
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Man9GlcNAc1 oligosaccharide
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl alpha-D-mannopyranoside
UMP + methyl (6-O-alpha-N-acetyl-D-glucosaminylphospho)-alpha-D-mannopyranoside
show the reaction diagram
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
show the reaction diagram
UDP-N-acetyl-D-glucosamine + NPC2
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
UMP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + pro-tripeptidyl peptidase
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ribonuclease B
UMP + ?
show the reaction diagram
UDP-N-acetyl-D-glucosamine + RNase B
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + soybean agglutinin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + thyroglobulin
UMP + ?
show the reaction diagram
-
weak activity
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-glucose
UMP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin
UMP + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-glucosamine + lysosomal-cathepsin Z D-mannose
UMP + lysosomal-cathepsin Z N-acetyl-D-glucosaminyl-phospho-D-mannose
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Man)5GlcNAc
-
-
(Man)7GlcNAc
-
-
ADP
-
5 mM, 39% inhibition
ATP
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5 mM, 59% inhibition
cathepsin D
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deglycosylated cathepsin D inhibits the activity of both forms of GlcNAc-1-phosphotransferase toward cathepsin D
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EDTA
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10 mM, complete inhibition
methyl-alpha-D-mannoside
-
-
NaCl
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0.1 M, 36% inhibition. 0.5 M, 91% inhibition
p-nitrophenyl-alpha-D-mannoside
-
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phosphatidic acid
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phosphatidylglycerol
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phosphatidylserine
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Sodium phosphate
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5 mM, pH 7.0, 55% inhibition
UDPGlcNAc
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UDPglucose
UTP
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5 mM, 34% inhibition
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-glucose 6-phosphate
-
activates
D-mannose 6-phosphate
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activates
Tergitol NP-10
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required
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.018 - 0.025
cathepsin D
-
0.03 - 0.06
DNase I
-
3.3 - 5.7
Man9GlcNAc1 oligosaccharide
33 - 48
methyl alpha-D-mannopyranoside
0.021 - 183
methyl-alpha-D-mannoside
0.352 - 0.367
NPC2
-
0.11
pro-tripeptidyl peptidase
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pH 7.4, 37C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37C, alpha2beta2 GlcNAc-1-phosphotransferase
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0.916 - 1.244
ribonuclease B
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0.5 - 0.556
RNase B
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1
soybean agglutinin
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pH 7.4, 37C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37C, alpha2beta2 GlcNAc-1-phosphotransferase
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0.021 - 0.2
UDP-GlcNAc
0.022 - 0.065
uteroferrin
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 0.11
cathepsin D
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0.0045 - 0.005
DNase I
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0.75 - 1.55
Man9GlcNAc1 oligosaccharide
0.5 - 0.75
methyl alpha-D-mannopyranoside
0.44 - 0.62
NPC2
-
0.008 - 0.038
pro-tripeptidyl peptidase
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0.042 - 0.05
RNase B
-
0.0041 - 0.005
soybean agglutinin
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0.011 - 0.033
uteroferrin
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 4.45
cathepsin D
-
0.08 - 0.15
DNase I
-
0.23 - 0.266
Man9GlcNAc1 oligosaccharide
0.0166
methyl alpha-D-mannopyranoside
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pH 7.4, 37C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37C, alpha2beta2 GlcNAc-1-phosphotransferase
1.25 - 1.7
NPC2
-
0.075 - 0.36
pro-tripeptidyl peptidase
-
0.09
RNase B
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pH 7.4, 37C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37C, alpha2beta2 GlcNAc-1-phosphotransferase
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0.005
soybean agglutinin
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pH 7.4, 37C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37C, alpha2beta2 GlcNAc-1-phosphotransferase
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0.45 - 1
uteroferrin
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.733
UDPglucose
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pH 7.6
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000038
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-
0.000733
-
-
0.12
-
-
6.82
-
after purification
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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with Tris-HCl giving 50% more activity than sodium cacodylate
6.6 - 7.5
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-
7.2 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
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pH 5.5: about 50% of maximal activity, pH 8.5: about 75% of maximal activity
6 - 9
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about 50% of maximal activity at pH 6 and at pH 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
20C: about 50% of maximal activity, 40C: about 25% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
no activity in fibroblasts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
gamma subunit is localised in the cis-Golgi apparatus
-
Manually annotated by BRENDA team
-
integral membrane protein
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36000
-
SDS-PAGE
41000
-
-
51000
-
2 * 166000 + 2 * 51000 + 2 * 56000, a 540000 Da enzyme complex is composed of disulfide-linked homodimers of 166000 and 51000 Da subunits and two identical, noncovalently associated 56000 Da subunits, SDS-PAGE
56000
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2 * 166000 + 2 * 51000 + 2 * 56000, a 540000 Da enzyme complex is composed of disulfide-linked homodimers of 166000 and 51000 Da subunits and two identical, noncovalently associated 56000 Da subunits, SDS-PAGE
145000
-
-
166000
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2 * 166000 + 2 * 51000 + 2 * 56000, a 540000 Da enzyme complex is composed of disulfide-linked homodimers of 166000 and 51000 Da subunits and two identical, noncovalently associated 56000 Da subunits, SDS-PAGE
176000
-
SDS-PAGE
190000
228000
-
enzyme from placenta, radiation inactivation
270000
-
alpha2beta2 GlcNAc-1-phosphotransferase
283000
-
enzyme from skin fibroblasts, radiation inactivation
330000
-
alpha2beta2gamma2 GlcNAc-1-phosphotransferase
1000000
-
-
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 190000, inactive mutant alphabeta precursor, SDS-PAGE, x * 45000, K4Q mutant beta subunit, SDS-PAGE, x * 41000, S15Y mutant beta subunit, SDS-PAGE
dimer
-
2 * 36000
heterodimer
heterohexamer
-
alpha2beta2gamma2
hexamer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 22
-
16 h, less than 20% loss of activity
37
-
2 h, less than 20% loss of activity
50
-
10 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
treatment with papain or phospholipase C from Bacillus cereus inactivates the enzyme in a time- and dose-dependent manner
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0C, 2 months, less than 10% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
HPC4-Sepharose column chromatography and DEAE-Sepharose column chromatography
-
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha2beta2gamma2 and alpha2beta2 GlcNAc-1-phosphotransferase are stably expressed in CHO-K1 cells (transmembrane segments are missing)
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cloning of a single cDNA and gene that encodes a precursor of the alpha- and beta-subunits of human GlcNAc-phosphotransferase (gene symbol, GNPTAB). Transfection of the alpha/beta-subunits precursor cDNA with or without cotransfection of the regulatory gamma-subunitc DNA results in an increase in GlcNAc-phosphotransferase activity on low molecular weight substrate. This demonstrates that the alpha/beta-subunits precursor cDNA encodes the catalytic domain of the enzyme
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expressed in 293-T cells
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expressed in CHO-K1 cells
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expressed in Escherichia coli
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expressed in Escherichia coli, COS-7 cells and HeLa cells
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gamma subunit is over-expressed in COS-7 cells
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gene GNPTAB encodes the alpha- and beta-subunits of GlcNAc-1-phosphotransferase, low efficiency of GNPTAB mRNA expression due to its large size
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gene GNPTAB encodes the alpha/beta-subunit of GlcNAc-1-phosphotransferase, recombinant expression of C-terminally V5/His-tagged wild-type and mutant enzymes in HEK293 cells
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gene GNPTAB, the alphabeta precursors of wild-type, and mutant K4Q or S15Y enzymes with a C-terminal V5-tag are expressed in HEK-293 cells
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gene GNPTG encoding the gamma-subunit of the enzyme, transient expression of wild-type and mutant gamma-subunits in HeLa cells
gene GNTPAB encoding the alpha/beta-subunits, quantitative real-time PCR expression analysis, recombinant expression of nucleotides 8-3715
genes GNPTABG encode the alpha2beta2gamma2 enzyme, generation of generate alpha/beta and gamma bicistronic constructs, recombinant expression of HA-tagged wild-type and GNPTAB-/- and GNPTG-/- mutant enzymes in HeLa cells, recombinant expression of domain deletion mutants in HEK-293 cells
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overexpression of gamma-chain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase in NIH-3T3 cells induces accumulation of macromolecules, formation of large cytoplasmic vacuoles and decrease of lysosomal enzymes in cells. Transient ectopic expression of the gamma subunit in endoplasmic reticulum induces lowered lysosomal enzyme activity in cells
plasmids encoding WT and K732N alpha/beta cDNA with C-terminal V5/His tags are generated and transfected into HEK-293 cells and monitoring of the proteolytic cleavage of the alpha/beta precursor by the appearance of the mature V5-tagged beta-subunit. Recombinant expression of wild-type and mutant GST-DMAP domain
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recombinant expression of C-terminally myc-tagged wild-type and mutant enzymes in HEK-293 cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C447Y
-
site-directed mutagenesis, the mutation does not affect the catalytic activity of the GlcNAc-1-phosphotransferase. Enzyme-deficient embryos rescued with C447Y mRNA only corrects 84% of mutational features, and embryos rescued with the mutant mRNA appear visually different, i.e. shorter, from embryos rescued with wild-type mRNA
C473S
-
site-directed mutagenesis, the mutation does not affect the catalytic activity of the GlcNAc-1-phosphotransferase. Enzyme-deficient embryos rescued with C473S mRNA only corrects 80% of mutational features, and embryos rescued with the mutant mRNA appear visually different, i.e. shorter, from embryos rescued with wild-type mRNA
A592T
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site-directed mutagenesis, mutation involved in enzyme dysfunction, that has no effect on the mutant enzyme
A955V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
A955V/K928R
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
C142S
-
mutant expressed as dimer
C142Y
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
C157S
-
mutant expressed as dimer
C157S/C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer
C169S
-
mutant expressed as dimer
C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer. Mutant is localised in the Golgi apparatus, indicating that dimerization is not essential for endoplasmic reticulum exit of the gamma-subunit. Monomeric C245S mutant does not assemble with endogenous GlcNAc-1-phosphotransferase 1 subunits
C442Y
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C461G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C468S
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C523R
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
C84S
-
mutant expressed as dimer
C84S/C157S
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mutant expressed as dimer
C84S/C157S/C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer
D1018G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
D190V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
D407A
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant in the Stealth domain trafficks to the Golgi
D407A/A663G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
F374L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
G106S
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
G126S
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
G575R
-
naturally occuring missense mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant shows 3% of wild-type activity
H956Y
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
I348L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant behaves similar to the wild-type enzyme
K1236A/R1237A/K1238A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
K1236M
L1001P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant partially exits from the endoplasmic reticulum and is almost inactive
L1054V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
L5A/L6A
-
replacement of the N-terminal dileucine motif with alanine residues results in a significant reduction of the PT alpha/beta-subunit precursor protein cleavage. Densitometric evaluation of intensities of immunoreactive bands show that the formation of the beta-subunit is reduced by 46% compared with the wild-type construct. Mutant mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
L5A/L6A/R1253A/I1254A/R1255A
-
double mutant containing a mutation of N-terminal and C-terminal endoplasmic reticulum export motif shows a strong inhibitory effect on cleavage of the PT alpha/beta-subunit precursor protein. Mutation leads to retention in the endoplasmic reticulum
L5A/L6A/R1253L/I1254L/R1255X
-
the transfer of the dileucine motif to the C-terminal domain replacing the dibasic-based motif 1253RIR1255 in combination with the substitution of the N-terminal dileucine motif, blocks the endoplasmic exit and the subsequent proteolytic cleavage to mature PT beta-subunit
L5R/L6R/R1253A/I1254A/R1255A
-
substitution of the N-terminal L-Leu/L-Leu motif by dibasic-based motifs RIR or RR in combination with alanine substitution of the C-terminal motif prevents the alpha/beta-subunit precursor protein from reaching the Golgi apparatus for cleavage
L785W
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the DMAP interaction domain mutation has full activity toward alpha-MM but impaired ability to phosphorylate lysosomal acid hydrolases
N1153S
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
N115Q
-
electrophoretic migration similar to wild-type at 34 kDa, mutant sensitive to PNGase F treatment
N88Q
-
electrophoretic migration similar to wild-type at 34 kDa, mutant sensitive to PNGase F treatment
N88Q/N115Q
-
electrophoretic migration at 31 kDa, double mutant insensitive to PNGase F treatment, non-glycosylated polypeptide. Non-glycosylated gamma-subunits do not colocalize with the Golgi apparatus marker GM130
Q926P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
R1242A/R1243A/R1244A
-
by mutation of the arginine motif in beta subunit it is shown that this signal is not a functional endoplasmic reticulum retention signal
R1244A/R1245A/R1246A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
R1253A/I1254A/R1255A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
R334L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant fails to exit from the endoplasmic reticulum and is inactive
R334Q
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant fails to exit from the endoplasmic reticulum and is inactive
R587P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the R587P mutant shifts from a predominant endoplasmic reticulum localization to a predominant Golgi localization
R925A
-
mutation results in an uncleavable PT alpha/beta-subunit precursor protein. Mutant co-localizes mainly with the cis-Golgi marker protein, no detection in endoplasmic reticulum
R986C
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant in the Stealth domain trafficks to the Golgi
S15Y
-
naturally occurring mutation in the N-terminal cytoplasmic tail of the alpha-subunit leading to a mislocated enzyme, mistargeting of the mutant enzymes to lysosomes, where they are degraded, or to the cell surface and release into the medium, but the mutant enzyme shows 41% of wild-type activity. Half-life of the mutant is decreased compared to the wild-type enzyme
T1223del
-
naturally occurig heterozygous mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant T1223del is correctly transported and proteolytically cleaved into mature alpha- and beta-subunits exhibiting 85% of GlcNAc-1-phosphotransferase activity of the wild-type enzyme
T286M
naturally occuring mutation of the gamma-subunit that does not alter the gamma-subunit function, the mutant variant enters the Golgi like the wild-type enzyme
T644M
-
naturally occuring heterozygous mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant T644M is correctly transported and proteolytically cleaved into mature alpha- and beta-subunits exhibiting 50% of GlcNAc-1-phosphotransferase activity of the wild-type enzyme
V182D
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
V182D/Q205P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
W81L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, that has no effect on the mutant enzyme
DELTA1-47
-
N-terminal region (residues 1-47) of Saccharomyces cerevisiae Alg14 localizes its green fluorescent protein fusion to the endoplasmic reticulum membrane. Coimmunoprecipitation demonstrates that the N-terminal region of Alg14 is required for direct interaction with Alg7
G163A/G165A
-
mutant fails to rescue a loss of Alg14 function. Mutant is inactivated by loss of conserved G-loop
V131A/I135A/V139A/V143A/V146A/F150A
-
a mutant in which six hydrophobic residues are replaced with L-Ala is able to rescue the loss of Alg14 function, indicating that the mutated hydrophobic residues do not have a deleterious effect on Alg14 activity. Growth of these cells is extremely slow at 30C
V131I/I135L/V139I/V143I/V146I/F150L
-
a mutant in which six hydrophobic residues are replaced with L-Ala is able to rescue the loss of Alg14 function
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
AAV-mediated expression of gene GNPTAB in mucolipidosis II, ML II, mice can attenuate bone loss via inhibition of IL-6 production