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1-palmitoyl lysophosphatidylcholine + H2O
glycerophosphocholine + palmitate
-
-
-
?
4-methylumbelliferyl 6-deoxy-6-thiopalmitoyl-beta-D-glucopyranoside + H2O
4-methylumbelliferyl 6-deoxy-6-thio-beta-D-glucopyranoside + palmitate
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 4-methylumbelliferyl 6-thio-beta-D-glucoside
5-bromo-4-chloro-3-indol-6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 5-bromo-4-chloro-3-indol-6-thio-beta-D-glucoside
-
-
-
-
?
myristoyl-CoA + H2O
myristate + CoA
-
-
-
-
?
palmitoyl-(alpha-subunit of the heterotrimeric G protein) + H2O
palmitic acid + alpha-subunit of the heterotrimeric G protein
-
-
-
-
?
palmitoyl-CoA + H2O
palmitate + CoA
palmitoyl-H-Ras + H2O
palmitate + Ha-Ras
palmitoyl-peptide + H2O
palmitate + peptide
residue 3 to 14 of RGS4 protein with palmitoyl group attached at Cys12 of RGS4 protein
-
-
?
palmitoyl-[MfNACsa protein] + H2O
palmitate + MfNACsa protein
-
substrate of isoform APT1
-
-
r
palmitoyl-[protein] + H2O
palmitate + protein
palmitoylthio-beta-glucoside + H2O
palmitate + thio-beta-glucoside
-
-
-
?
palmitoyl[beta-D-thioglucoside] + H2O
palmitate + 1-thio-beta-D-glucopyranose
-
-
-
-
?
S-palmitoyl-N-acetyl-O-carboxymethyl-cysteine + H2O
N-acetyl-O-carboxymethyl-cysteine + palmitate
-
enzyme form PPT1, not PPT2
-
?
S-palmitoyl-N-acetylcysteamine + H2O
N-acetylcysteamine + palmitate
-
enzyme form PPT1, not PPT2
-
?
additional information
?
-
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
4MU-6S-palm-beta-Glc
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
Drosophila sp. (in: flies)
-
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
artificial substrate
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
artificial substrate
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 4-methylumbelliferyl 6-thio-beta-D-glucoside
-
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 4-methylumbelliferyl 6-thio-beta-D-glucoside
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 4-methylumbelliferyl 6-thio-beta-D-glucoside
-
-
-
-
?
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
palmitate + 4-methylumbelliferyl 6-thio-beta-D-glucoside
-
-
-
?
palmitoyl-CoA + H2O
palmitate + CoA
-
-
-
-
?
palmitoyl-CoA + H2O
palmitate + CoA
-
-
-
?
palmitoyl-CoA + H2O
palmitate + CoA
-
preferred substrate of PPT2
-
?
palmitoyl-H-Ras + H2O
palmitate + Ha-Ras
-
the enzyme recognizes H-Ras as substrate only when H-Ras is in its native conformation
-
-
?
palmitoyl-H-Ras + H2O
palmitate + Ha-Ras
-
palmitate-labeled, histidine-tagged H-Ras
-
-
?
palmitoyl-H-Ras + H2O
palmitate + Ha-Ras
-
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
various S-acylated proteins
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
palmitoylation plays critical roles in diverse biological functions, including membrane anchorage, vesicular transport, signal transduction and the maintenance of cellular architecture
-
-
r
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
palmitoylation plays critical roles in diverse biological functions, including membrane anchorage, vesicular transport, signal transduction and the maintenance of cellular architecture
-
-
r
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
hydrolysis of long-chain fatty acids from S-acylated proteins and CoA
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
hydrolysis of long-chain fatty acids from S-acylated proteins and CoA
-
?
additional information
?
-
-
no effect on palmitoylation of endothelial nitric oxide synthase
-
-
?
additional information
?
-
-
altough the ppt-1 gene is not essential for the animals survival, its mutation results in a mild developmental and reproductive phenotype, affects the number and size of mitochondria and results in an abnormality in mitochondrial morphology
-
-
?
additional information
?
-
-
depalmitoylation reaction, palmitoylation is the post-translational addition of a palmitate moiety to a cysteine residue through a covalent thioester bond
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
Ppt1 modulates the activity of several pathways known to play a role in synaptic development either directly through its depalmitoylation activity or indirectly through effects on general endocytic mechanisms
-
-
?
additional information
?
-
-
enzyme assay development
-
?
additional information
?
-
-
structural differences in the 2 enzyme fomrs PPT1 and PPT2, PPT2 does not hydrolyze substrates with bulky head groups
-
?
additional information
?
-
-
mutations in the enzyme protein cause the neurodegenerative disorder infantile neuronal ceroid lipofuscinosis
-
-
?
additional information
?
-
-
defect in the palmitoyl-(protein) hydrolase gene causes a neurodegenerative disorder. Depalmitoylation of the still uncharacterized substrate(s) of the enzyme is critical for postnatal development or maintainance of cortical neurons
-
-
?
additional information
?
-
-
the enzyme is required for the efficient lysosomal degradation of thioesters derived from S-acylated proteins
-
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological and granular osmiophilic deposits, GROD, and infantile neuronal ceroid lipofuscinosis
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, a lysosomal storage disorder
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, molecular basis
-
?
additional information
?
-
-
enzyme deficiency causes the infantile form of neuronal ceroid lipofuscinosis INCL, a progressive encephalopathyof children
-
?
additional information
?
-
-
PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
PPT1 deficiency causes, together with tripeptidyl peptidase 1 deficiency, progressive neurological disorder infantile neuronal ceroid lipofuscinosis, a group of at least 8 inherited, progressive encephalopathies that are characterized by lipofuscin-like inclusions in various tissues and have been classified as CNL1-CNL8
-
?
additional information
?
-
the most severe form of neuronal ceroid lipofuscinoses, infantile neuronal ceroid lipofuscinosis (INCL), is caused by mutations in the CLN1 gene, resulting in a deficiency of the lysosomal enzyme, palmitoyl protein thioesterase 1
-
-
?
additional information
?
-
-
PPT1 deficiency leads to abnormally low levels of soluble synaptic vesicle proteins like synaptobrevin 2 and SNAP25, that are known to undergo palmitoylation and are critical for fusion, exocytosis, recycling, and regeneration of fresh synaptic vesicles
-
-
?
additional information
?
-
-
PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, only in neurons of the cerebral and cerbellar cortexes and retina not in other cell types, characterized by early loss of vision and massiv neuronal death
-
?
additional information
?
-
-
the enzyme has a role outside the lysosome in the brain and might be associated with synaptic functioning
-
?
additional information
?
-
-
in palmitoyl-protein thioesterase-1-knockout mice (that mimic human infantile neuronal ceroid lipofuscinosis) the endoplasmic reticulum in the brain cells is structurally abnormal. Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in human infantile neuronal ceroid lipofuscinosis
-
-
?
additional information
?
-
-
PPT1 deficiency leads to abnormally low levels of soluble synaptic vesicle proteins like synaptobrevin 2 and SNAP25, that are known to undergo palmitoylation and are critical for fusion, exocytosis, recycling, and regeneration of fresh synaptic vesicles
-
-
?
additional information
?
-
-
enzyme deficiency causes infantile neuronal ceroid lipofuscinosis, the enzyme plays an important role in the development of the CNS
-
?
additional information
?
-
-
epileptic seizures in adult rats lead to progressive and remarkable increase in enzyme activity inlimbic areas of the brain, the enzyme may protect neurons from excitotoxicity and have a role in synaptic plasticity, enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
the enzyme is essential for both development and maintenance of cortical neurons, enzyme deficiency causes severe neurodegenerative disorders by loss of cortical neurons
-
?
additional information
?
-
PPT1 mutations cause severe neurodegenerative storage disorder, termed infantile Batten, in humans, Schizosaccharomyces pombe is a genetically tractable model for the sutdy of this disease due to evolutionary highly conserved gene and function
-
?
additional information
?
-
-
PPT1 mutations cause severe neurodegenerative storage disorder, termed infantile Batten, in humans, Schizosaccharomyces pombe is a genetically tractable model for the sutdy of this disease due to evolutionary highly conserved gene and function
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
palmitoyl-[protein] + H2O
palmitate + protein
additional information
?
-
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
palmitoylation plays critical roles in diverse biological functions, including membrane anchorage, vesicular transport, signal transduction and the maintenance of cellular architecture
-
-
r
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
-
-
?
palmitoyl-[protein] + H2O
palmitate + protein
-
palmitoylation plays critical roles in diverse biological functions, including membrane anchorage, vesicular transport, signal transduction and the maintenance of cellular architecture
-
-
r
additional information
?
-
-
no effect on palmitoylation of endothelial nitric oxide synthase
-
-
?
additional information
?
-
-
altough the ppt-1 gene is not essential for the animals survival, its mutation results in a mild developmental and reproductive phenotype, affects the number and size of mitochondria and results in an abnormality in mitochondrial morphology
-
-
?
additional information
?
-
-
depalmitoylation reaction, palmitoylation is the post-translational addition of a palmitate moiety to a cysteine residue through a covalent thioester bond
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
Ppt1 modulates the activity of several pathways known to play a role in synaptic development either directly through its depalmitoylation activity or indirectly through effects on general endocytic mechanisms
-
-
?
additional information
?
-
-
mutations in the enzyme protein cause the neurodegenerative disorder infantile neuronal ceroid lipofuscinosis
-
-
?
additional information
?
-
-
defect in the palmitoyl-(protein) hydrolase gene causes a neurodegenerative disorder. Depalmitoylation of the still uncharacterized substrate(s) of the enzyme is critical for postnatal development or maintainance of cortical neurons
-
-
?
additional information
?
-
-
the enzyme is required for the efficient lysosomal degradation of thioesters derived from S-acylated proteins
-
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological and granular osmiophilic deposits, GROD, and infantile neuronal ceroid lipofuscinosis
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, a lysosomal storage disorder
-
?
additional information
?
-
-
enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, molecular basis
-
?
additional information
?
-
-
enzyme deficiency causes the infantile form of neuronal ceroid lipofuscinosis INCL, a progressive encephalopathyof children
-
?
additional information
?
-
-
PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
PPT1 deficiency causes, together with tripeptidyl peptidase 1 deficiency, progressive neurological disorder infantile neuronal ceroid lipofuscinosis, a group of at least 8 inherited, progressive encephalopathies that are characterized by lipofuscin-like inclusions in various tissues and have been classified as CNL1-CNL8
-
?
additional information
?
-
the most severe form of neuronal ceroid lipofuscinoses, infantile neuronal ceroid lipofuscinosis (INCL), is caused by mutations in the CLN1 gene, resulting in a deficiency of the lysosomal enzyme, palmitoyl protein thioesterase 1
-
-
?
additional information
?
-
-
PPT1 deficiency leads to abnormally low levels of soluble synaptic vesicle proteins like synaptobrevin 2 and SNAP25, that are known to undergo palmitoylation and are critical for fusion, exocytosis, recycling, and regeneration of fresh synaptic vesicles
-
-
?
additional information
?
-
-
PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, only in neurons of the cerebral and cerbellar cortexes and retina not in other cell types, characterized by early loss of vision and massiv neuronal death
-
?
additional information
?
-
-
the enzyme has a role outside the lysosome in the brain and might be associated with synaptic functioning
-
?
additional information
?
-
-
in palmitoyl-protein thioesterase-1-knockout mice (that mimic human infantile neuronal ceroid lipofuscinosis) the endoplasmic reticulum in the brain cells is structurally abnormal. Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in human infantile neuronal ceroid lipofuscinosis
-
-
?
additional information
?
-
-
PPT1 deficiency leads to abnormally low levels of soluble synaptic vesicle proteins like synaptobrevin 2 and SNAP25, that are known to undergo palmitoylation and are critical for fusion, exocytosis, recycling, and regeneration of fresh synaptic vesicles
-
-
?
additional information
?
-
-
enzyme deficiency causes infantile neuronal ceroid lipofuscinosis, the enzyme plays an important role in the development of the CNS
-
?
additional information
?
-
-
epileptic seizures in adult rats lead to progressive and remarkable increase in enzyme activity inlimbic areas of the brain, the enzyme may protect neurons from excitotoxicity and have a role in synaptic plasticity, enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL
-
?
additional information
?
-
-
the enzyme is essential for both development and maintenance of cortical neurons, enzyme deficiency causes severe neurodegenerative disorders by loss of cortical neurons
-
?
additional information
?
-
PPT1 mutations cause severe neurodegenerative storage disorder, termed infantile Batten, in humans, Schizosaccharomyces pombe is a genetically tractable model for the sutdy of this disease due to evolutionary highly conserved gene and function
-
?
additional information
?
-
-
PPT1 mutations cause severe neurodegenerative storage disorder, termed infantile Batten, in humans, Schizosaccharomyces pombe is a genetically tractable model for the sutdy of this disease due to evolutionary highly conserved gene and function
-
?
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A179T
Drosophila sp. (in: flies)
-
loss-of-function allele, although endocytosis and endo-lysosomal trafficking does occur in Ppt1 mutant garland cells, there is a reduced level of uptake and a decreased rate of trafficking to the lysosomes
S77F
Drosophila sp. (in: flies)
-
loss-of-function allele, although endocytosis and endo-lysosomal trafficking does occur in Ppt1 mutant garland cells, there is a reduced level of uptake and a decreased rate of trafficking to the lysosomes
C6S
the activity of the non-palmitoylatable mutant significantly surpasses that of the wild type enzyme by more than 42% in the cell lysate and 25% in the cell medium
D233N
-
site-directed mutagenesis, inactive mutant
E184K
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with the infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
F84del
-
natural deletion mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
G118D
-
natural mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
G250V
-
naturally occurring mutation, recombinant enzyme shows 5.9% of the wild-type activity, mutation is associated with the juvenile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
G42E
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with the infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
H289A
-
site-directed mutagenesis, inactive mutant
H39Q
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with the infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
L219Q
-
naturally occurring mutation, mutation is associated with the late onset form of infantile neuronal ceroid lipofuscinosis, the mutant enzymes shows minor altered intracellular localization in transfected cells and are localized in the presynaptic space and neuronal shaft, about 10fold reduced activity
N197Q
-
site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity
N197Q/N212Q
-
site-directed mutagenesis, mutation of glycosylation sites, slightly reduced activity, mutant shows 10% of the wild-type expression level
N197Q/N212Q/N232Q
-
site-directed mutagenesis, mutation of all glycosylation sites, inactive mutant
N197Q/N232Q
-
site-directed mutagenesis, mutation of glycosylation sites, reduced activity
N212Q
-
site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity
N212Q/N232Q
-
site-directed mutagenesis, mutation of glycosylation sites, highly reduced activity
N232Q
-
site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity
Q291X
-
natural mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
R122W
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with the infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor, accumulation of the recombinant mutant enzyme in the endoplamic reticulum due to decreased degradation turnover
R164X
-
natural mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
S115A
-
site-directed mutagenesis, inactive mutant
S119A
part of the catalytic triad, no activity
S199A
mutation shows 1-5% of normal activity
S199A/S214A
mutant enzyme with very low enzyme activity
S214A
mutant shows 31% of normal activity
S234A
mutation shows 1-5% of normal activity. Partial localization to lysosomes, although a major proportion is retained in the endoplasmic reticulum
Y109D
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with an unclassified form of neuronal ceroid lipofuscinosis
Y247H
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with an unclassified form of neuronal ceroid lipofuscinosis
A179T
-
loss-of-function allele
A179T
loss-of-function mutant, shows an increased frequency of mini excitatory junctional potentials, defects in vesicle cycling during and following repetitive stimulation, and a decreased rate of fluorescent endocytic tracer FM1-43 endocytosis
S77F
-
loss-of-function allele
S77F
loss-of-function mutant, shows an increased frequency of mini excitatory junctional potentials, defects in vesicle cycling during and following repetitive stimulation, and a decreased rate of fluorescent endocytic tracer FM1-43 endocytosis
D79G
-
site-directed mutagenesis, highly reduced activity
D79G
-
naturally occurring mutation, recombinant enzyme shows 32.8% of the wild-type activity, mutation is associated with the juvenile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
Q177E
-
natural missense mutation in gene ppt1, leading to enzyme deficiency and progressive neurological defects, late-infantile phenotype
Q177E
-
naturally occurring mutation, recombinant enzyme shows 7.3% of the wild-type activity, mutation is associated with the late infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
T75P
-
site-directed mutagenesis, highly reduced activity
T75P
-
natural mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
T75P
-
naturally occurring mutation, mutation is associated with the late onset form of infantile neuronal ceroid lipofuscinosis, the mutant enzymes shows minor altered intracellular localization in transfected cells and are localized in the presynaptic space and neuronal shaft, about 10fold reduced activity
T75P
-
naturally occurring mutation, recombinant enzyme shows 6.8% of the wild-type activity, mutation is associated with the juvenile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
V181M
-
natural mutation in gene ppt1, leading to enzyme deficiency and infantile progressive neurological defects
V181M
-
naturally occurring mutation, recombinant enzyme is nearly inactive showing an activity below 2% of the wild-type activity, mutation is associated with the infantile form of neuronal ceroid lipofuscinosis, no binding of mannose 6-phosphate receptor
additional information
-
naturally occurring mutations delPhe84 and insCys45, mutation is associated with the late onset form of infantile neuronal ceroid lipofuscinosis, the mutant enzymes shows severely altered intracellular localization in transfected cells and are targeted to the endoplasmic reticulum, about 10fold reduced activity
additional information
-
residues involved in ligand binding differ between PPT1 and PPT2, exchange by site-directed mutagenesis and functional analysis, overview
additional information
-
several naturally occurring mutations of alleles 1 and 2 from enzyme deficient patients shows reduced activity compred with the wild-type, overview
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Rattus norvegicus (P45479)
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Homo sapiens
-
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Homo sapiens (P50897), Homo sapiens
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Mus musculus
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Homo sapiens (P50897), Homo sapiens
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