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Information on EC 3.1.2.22 - palmitoyl[protein] hydrolase
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3.1.2.22 palmitoyl[protein] hydrolaseIUBMB Comments
Specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.
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Word Map
- 3.1.2.22
-
ceroid
-
infantile
- lipofuscinosis
-
palmitoylated
- lysosomal
- neurodegenerative
- batten
-
depalmitoylation
-
ppt1-deficient
-
autofluorescent
-
grods
-
tripeptidyl
-
osmiophilic
-
s-acylated
-
late-infantile
-
lincl
-
thioesterases
-
lipid-modified
- ceroid-lipofuscinosis
- medicine
- nutrition
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
palmitoyl-protein thioesterase, palmitoyl-protein thioesterase 1, palmitoyl protein thioesterase, palmitoyl protein thioesterase 1, palmitoyl-protein thioesterase-1, palmitoyl protein thioesterase-1, acyl-protein thioesterase 1, lysophospholipase 1, palmitoyl protein thioesterase-2, palmitoyl-thioesterase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acyl protein thioester hydrolase
-
-
-
-
CLN1
G14
-
-
-
-
GenBank AF020543-derived protein GI 2501961
-
-
-
-
GenBank L42809-derived protein GI 1160967
-
-
-
-
Hydrolase, acyl protein thioester
-
-
-
-
Hydrolase, acyl protein thioester (cattle clone pBovPPT-18 precursor reduced)
-
-
-
-
Hydrolase, acyl protein thioester (cattle pBovPPT-25 precursor reduced)
-
-
-
-
Hydrolase, acyl protein thioester (human clone B lysosome-associated isoenzyme 2)
-
-
-
-
Hydrolase, acyl protein thioester (human clone pHuPPT-5')
-
-
-
-
Hydrolase, acyl protein thioester (ox clone pBovPPT-18 precursor reduced)
-
-
-
-
Hydrolase, acyl protein thioester (ox pBovPPT-25 precursor reduced)
-
-
-
-
Hydrolase, acyl protein thioester (rat clone pRatPPT-44 precursor reduced)
-
-
-
-
palmitoyl protein thioesterase
palmitoyl protein thioesterase 1
palmitoyl protein thioesterase-1
Palmitoyl-protein thioesterase
Palmitoyl-protein thioesterase (bovine clone pBovPPT-17 precursor)
-
-
-
-
Palmitoyl-protein thioesterase (bovine clone pBovPPT-25 precursor)
-
-
-
-
Palmitoyl-protein thioesterase (human clone pHuPPT-5')
-
-
-
-
Palmitoyl-protein thioesterase (rat clone pRatPPT-44 precursor)
-
-
-
-
palmitoyl-protein thioesterase 1
Palmitoyl-protein thioesterase PPT2 (human clone B lysosome associated)
-
-
-
-
palmitoyl-protein thioesterase-1
PPT
PPT1
Palmitoyl-protein thioesterase
-
-
-
-
PPT
-
-
-
-
PPT1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl[protein] + H2O = palmitate + protein
-
-
-
-
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA
-
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA
-
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA
-
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA, catalytic triad consists of Ser115, His289, and Asp233
-
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA, catalytic triad of PPT2 consists of Ser111, His283, and Asp228, mechanism, both PPT1 and PPT2 have lipid-binding grooves leading away from the active site
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of thioester
hydrolysis of thioester
-
-
-
-
hydrolysis of thioester
-
-
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SYSTEMATIC NAME
IUBMB Comments
palmitoyl[protein] hydrolase
Specific for long-chain thioesters of fatty acids. Hydrolyses fatty acids from S-acylated cysteine residues in proteins, palmitoyl cysteine and palmitoyl-CoA.
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CAS REGISTRY NUMBER
COMMENTARY
150605-49-5
-
158210-90-3
hydrolase, acyl protein thioester (rat clone pRatPPT-44 precursor reduced) /palmitoyl-protein thioesterase (rat clone pRatPPT-44 precursor)
158210-92-5
hydrolase, acyl protein thioester (cattle clone pBovPPT-18 precursor reduced) /hydrolase, acyl protein thioester (ox clone pBovPPT-18 precursor reduced) /palmitoyl-protein thioesterase (bovine clone pBovPPT-17 precursor)
158210-93-6
hydrolase, acyl protein thioester (cattle pBovPPT-25 precursor reduced) /hydrolase, acyl protein thioester (ox pBovPPT-25 precursor reduced) /palmitoyl-protein thioesterase (bovine clone pBovPPT-25 precursor)
179801-10-6
hydrolase, acyl protein thioester (human clone pHuPPT-5') /GenBank L42809-derived protein GI 1160967 /palmitoyl-protein thioesterase (human clone pHuPPT-5')
199619-79-9
hydrolase, acyl protein thioester (human clone B lysosome-associated isoenzyme 2) /genBank AF020543-derived protein GI 2501961 /palmitoyl-protein thioesterase PPT2 (human clone B lysosome associated)
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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
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
-
-
-
-
?
palmitoyl-(alpha-subunit of the heterotrimeric G protein) + H2O
palmitic acid + alpha-subunit of the heterotrimeric G protein
-
-
-
-
?
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
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
-
?
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-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-[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
-
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
-
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
?
-
-
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.
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
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
-
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-palmitoyl lysophosphatidylcholine
competitive inhibitor for acylprotein thioesterase activity
Chloroquine
-
inhibits the hydrolysis and leads to accumulation of lipid cysteine thioesters in the lysosomes of treated cells
leupeptin
-
inhibits the hydrolysis and leads to accumulation of lipid cysteine thioesters in the lysosomes of treated cells but has no direct inhibitory effect on the enzyme
additional information
Drosophila sp. (in: flies)
-
dSmt3 mutations are the lone suppressor modifiers
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Drosophila sp. (in: flies)
-
Drosophila C-terminal Src kinase is an enhancer of the Ppt1 phenotype. Mutations in the fear of intimacy gene are also identified as enhancers. Mutations in zipper or mutations at the Drosophila IGF-II mRNA-binding protein locus enhance the degenerative phenotype. The tsg alleles tsg2 and tsg4 both enhance the rough eye phenotype produced by Ppt1 expression
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0222
1-palmitoyl lysophosphatidylcholine
for acylprotein thioesterase activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0055
substrate 4-methylumbelliferyl 6-deoxy-6-thiopalmitoyl-beta-D-glucopyranoside, cerebral cortex gray matter lysate, pH not specified in the publication, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain deleted for ppt-1, potentially provides a model system for the study of human infantile neuronal ceroid lipofuscinosis
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
exclusively localized to the basolateral side of the polarized cells
brenda
normal fibroblasts and infantile neuronal ceroid lipofuscinosis fibroblasts, deficient of PPT1
brenda
-
primary cortical neuron culture from tissue of PPT1 knockout mice that mimic infantile neuronal ceroid lipofuscinosis
brenda
additional information
-
postmortem from patient with infantile neuronal ceroid lipofuscinosis (INCL) caused by PPT1 deficiency
brenda
-
expression of enzyme is developmentally regulated, with increasing expression during maturation of the CNS, reaching the maximum in young adulthood
brenda
-
PPT1-/- cerebella appear smaller than aged matched wild-type littermates
brenda
additional information
-
the most common mutation results in intracellular accumulationof the enzyme polypeptide and undetectable activity in the brain
brenda
additional information
-
lymphoblasts from patients with infantile neuronal ceroid lipofuscinosis, deficient of PPT1
brenda
additional information
-
activity is increased during neuronal maturation
brenda
additional information
-
the enzyme expression is strictly developmentally regulated in brain and eyes but not in spleen
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the most common mutation results in intracellular accumulation of the enzyme polypeptide and undetectable activity in the brain
brenda
-
cortical, in synaptic junctions of epileptic rats, nearly not in non-epileptic ones
brenda
additional information
-
in contrast to the wild type enzyme, the mutant polypeptides are retained in the endoplasmic reticulum, most probably due to the misfolding of the mutant polypeptide
brenda
-
infantile neuronal ceroid lipofuscinosis is a lysosomal storage disease
brenda
-
enzyme is recognized by the mannose 6-phosphate receptor and routed to the lysosome
brenda
-
the glycoslated enzyme is recognized by the mannose 6-phosphate receptor and routed to the lysosome
brenda
additional information
-
colocalization of the enzyme with the synaptic membrane marker is enhanced after epileptic seizures
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
first case of infantile neuronal ceroid lipofuscinosis in 37 month old Japanese boy diagnosed by enzyme activity deficiency of palmitoyl-protein thioesterase, displaying symptoms of severe deterioration beginning in his 14th month
malfunction
Drosophila sp. (in: flies)
-
Garland cells from Ppt1 loss-of-function mutants have defects in endocytic trafficking
malfunction
PPT1 deficient cells are partially resistant to tumor necrosis factor-induced cell death (57-75% cell viability versus 15-30% for control fibroblasts), tumor necrosis factor-initiated proteolytic cleavage of caspase-8, Bid and caspase-3, as well as cytochrome c release is strongly attenuated. Activation of p42/p44 mitogen-activated protein kinase and of transcription factor NF-kappaB by tumor necrosis factor, and induction of cell death by staurosporine or chemotherapeutic drugs in infantile neuronal ceroid lipofuscinosis cells are unaffected by PPT1 deficiency
malfunction
-
PPT1-deficient mouse (PPT1-/-) mimics the clinical symptoms and underlying pathology of infantile neuronal ceroid lipofuscinosis: Purkinje cell loss beginning at 3 months, which correlates with changes in rotarod performance, an early stage reactive gliosis and a primary pathology in astrocytes, including changes in S100beta and GLAST expression, a late stage granule cell loss, microglial activation, and demyelination. Neuronalglial interactions are the core pathology in the PPT1-/- cerebellum
malfunction
-
resistance to tumor necrosis factor-induced apoptosis in embryonic fibroblasts derived from Ppt1/Cln1-deficient mice but not from mice with a targeted deletion of Cln3 or Cln5 (murine models of ceroid lipofuscinosis)
malfunction
neuronal ceroid lipofuscinoses-like signs caused by single nucleotide insertion in exon 8 (homozygous)
malfunction
enzyme deficiency causes alterations in the mitochondrial respiratory chain. Enzyme-deficient neurons are more sensitive to mitochondrial complex I inhibition by 1-methyl-4-phenylpyridinium and have significantly decreased sensitivity to chemical anoxia induced by the mitochondrial complex IV inhibitor sodium azide
physiological function
Drosophila sp. (in: flies)
-
Ppt1 plays a role in modulating the early stages of vesicle formation. There may be a connection between Ppt1 and bone morphogenetic protein signaling at the cellular level. Expression of wild-type Ppt1 in the adult visual system using GMR-Gal4 alters the external and internal organization of the adult retina. When co-expressed UAS-dynamin with Ppt1 there is a significant enhancement of the rough eye phenotype
physiological function
-
role of PPT1 and, likely, protein depalmitoylation in the regulation of tumor necrosis factor-induced apoptosis
physiological function
role of PPT1 and, likely, protein depalmitoylation in the regulation of tumor necrosis factor-induced apoptosis. PPT1 is involved in cell death triggered by death receptors but not receptor-independent cytotoxic agents. Expression of PPT1 cDNA in infantile neuronal ceroid lipofuscinosis cells restores the tumor necrosis factor sensitivity
physiological function
-
when injected intravenously into PPT1-deficient mice, the clearance of recombinant PPT1 from plasma is rapid, with a half-life of 10 min. Most of the injected dose is distributed to the kidney and liver and potentially corrective levels are also observed in heart, lung and spleen. Brain uptake is minimal. The enzyme is largely mannose 6-phosphorylated and takes up rapidly by PPT1-deficient immortalized lymphoblasts derived from infantile neuronal ceroid lipofuscinosis patients
physiological function
-
essential for proper neuronal cell fates and organization, ortholog to the human Batten disease palmitoyl protein thioesterase 1
physiological function
-
homozygous palmitoyl-protein thioesterase PPT1 knockout mice reproduce the known features of infantile neuronal ceroid lipofuscinosis, developing signs of motor dysfunction at 5 months of age and death by around 8 months. PPT1 knockout mice treated with purified recombinant PPT1 corresponding to 12 mg/kg or 180 U/kg for a 25 g mouse administered intravenously weekly either from birth or beginning at 8 weeks of age surprisingly well tolerate the treatment and neither anaphylaxis nor antibody formation is observed. In mice treated from birth, survival increases from 236 to 271 days and the onset of motor deterioration is similarly delayed. In mice treated beginning at 8 weeks, no increases in survival or motor performance are seen. Outside the central nervous system, substantial clearance of autofluorescent storage material in many tissues is observed. Macrophages in spleen, liver and intestine are especially markedly improved, as are acinar cells of the pancreas and tubular cells of the kidney
physiological function
mutations in palmitoyl-protein thioesterase Ppt1 genetically interact with temperature sensitive mutations in the Drosophila dynamin gene shibire, accelerating the paralytic behavior of shibire mutants at 27°C. Ppt1-deficient larvae show an increase in miniature excitatory junctional potentials and a significant depression of evoked excitatory junctional potentials in response to repetitive stimulation. In Ppt1-mutant larvae, there is a significant decrease in fluorescent endocytic tracer FM1-43 uptake at the mutant neuromuscular junction. Ppt1-deficient and Ppt1 point mutant larvae display defects in locomotion that are consistent with alterations in synaptic function
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
101000
x * 31000, processed enzyme, SDS-PAGE, x * 101000, unprocessed enzyme, SDS-PAGE
31000
x * 31000, processed enzyme, SDS-PAGE, x * 101000, unprocessed enzyme, SDS-PAGE
37000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 31000, processed enzyme, SDS-PAGE, x * 101000, unprocessed enzyme, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
enzyme contains 2 putative cleavage sites for the kex-related endopeptidase Krp1p, the precursor is proteolytically processed to form distinct Ppt1p and Dolpp1p domains, Arg354 is crucial for the processing
glycoprotein
-
heterogenous glycosylation is the major cause of multiple bands observed in SDS-PAGE
glycoprotein
three potential asparagine-linked glycosylation sites are found near the carboxyl terminus of the protein at positions 199, 214, and 234. Glycosylation of the amino acid 234 demonstrated experimentally
glycoprotein
-
N-glycosylation at Asn232, Asn197, and Asn212, essential for activity
glycoprotein
N-glycosylation of N197 and N232, but not N212, is essential for enzyme activity and intracellular transport. Deglycosylation of overexpressed PPT1 produced in neurons and fibroblasts demonstrates differentially modified PPT1 in different cell types
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme with and without bound palmitate, sitting drop vapor diffusion method, 12 mg/ml enzyme in 20 mM HEPES, pH 7.0, plus 150 mM NaCl, plus reservoir solution, containing 55% PEG 400, 100 mM Bis-Tris, pH 6.5, in a ratio 3:2, equilibrated against a250fold excess, X-ray multiwave length anomalous diffraction phasing for structure determinationand analysis, 2.25 A resolution
-
purified recombinant PPT2 15 mg/ml, sitting drop vapour diffusion method, 4°C, with equal volume of precipitant solution conataining 2 M ammonium sulfate, 100 mM sodium cacodylate, pH 5.5-6.5, 8% methyl pentanediol, X-ray diffraction structure determination and analysis at 2.7 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A179T
S77F
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
D79G
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
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
Q177E
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
S234A
mutation shows 1-5% of normal activity. Partial localization to lysosomes, although a major proportion is retained in the endoplasmic reticulum
T75P
V181M
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
additional information
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 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
-
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
-
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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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant PPT2 from overexpressing insect cells, recombinant PPT2 mutant from COS cells
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a UAS:GFP-Ppt1 transgenic fly line. The pUAST:GFP-Ppt1 vector overexpressed using Act5C-Gal4
Drosophila sp. (in: flies)
-
DNA sequence determination and analysis, enzyme is encoded in frame with a second gene coding for an indispensable dolichol pyrophosphatase, gene pdf1, strains bearing a deletion of the entire pdf1 open reading frame are nonviable, due to Dolpp1p deficiency, and are rescued by pdf1 expression plasmid, mutations only in the palmitoyl protein thioesterase 1 domain results in cells abnormally sensitive to sodium vanadate and elevated extracellular pH, the pdf1-deficient phenotype is complemented by the human PPT1 gene
expression as glutathione S-transferase fusion protein in BHK and CHO cells, localization of the recombinant enzyme out side the lysosomes and endosomes
-
expression of the enzyme in Caco-2 cells, orientation to the basolateral side, also after endocytosis of the recombinant enzyme into Caco-2 cells
-
expression of wild-type and enzymes with naturally occurring mutations in COS cells as His-tagged enzyme, and in Sf9 cells, the latter via baculovirus infection
-
fragment corresponding to the entire coding region of PPT1 amplified from pCMV5-hPPT1, and cloned into XhoI sites in the polylinker region of expression vector pMSXND1, overexpressed in CHO cells. PPT1 injected intravenously into PPT1-deficient mice
-
gene ppt, DNA sequence determnation and analysis, identification of 8 natural mutations of different origins leading to enzyme deficiency
-
GST-fusion protein expressed in Escherichia coli BL21, expressed in HEK-293 cell
overexpression of PPT2 in an insect-baculovirus expression system, secretion of the recombinant enzyme to the culture medium, expression of mutant PPT2 in COS cells, subcloning in Escherichia coli XL1-blue
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in rats fed a high-fat diet, palmitoyl-protein thioesterase PPT1 is upregulated. In a Sertoli-cell line cultured in a high-fat supplemented medium, PPT1 abundance Is accompanied by increases in the endocytic vesicle-associated protein, clathrin, and decreases in the tight junctional proteins, ZO-1 and occludin
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
the litter sizes for females mated to obese males are significantly lower as compared to females mated with normal-diet-fed controls. Their serum high-density lipoprotein, low-density lipoprotein, cholesterol, and estradiol levels increase in obese males, but testosterone and follicle-stimulating hormone levels decrease. Testicular morphology disruptions include Sertoli-cell atrophy, disrupted tight junctions, and mitochondrial degeneration in spermatogenic cells. In rats fed a high-fat diet, palmitoyl-protein thioesterase PPT1 is upregulated. In a Sertoli-cell line cultured in a high-fat supplemented medium, PPT1 abundance Is accompanied by increases in the endocytic vesicle-associated protein, clathrin, and decreases in the tight junctional proteins, ZO-1 and occludin
medicine
-
in vitro enzyme assay that can be readily used for the clinical diagnosis of both infantile neuronal ceroid lipofuscinosis patients and carrier
medicine
-
palmitoyl protein thioesterase 1, expressed in the human saliva is a reliable and non-invasive source for the diagnosis of infantile neuronal ceroid lipofuscinosis
medicine
-
enzyme may be useful as an adjunct to central nervous system-directed therapies and may be used as a starting point for modifications designed to improve brain delivery
medicine
-
if patients are diagnosed with any type of mental and/or physical retardation accompanied by strong and severe visual impairment, then the case physician may consider the possibility of infantile neuronal ceroid lipofuscinosis and conduct an examination of PPT activity level
medicine
-
homozygous palmitoyl-protein thioesterase PPT1 knockout mice reproduce the known features of infantile neuronal ceroid lipofuscinosis, developing signs of motor dysfunction at 5 months of age and death by around 8 months. PPT1 knockout mice treated with purified recombinant PPT1 corresponding to 12 mg/kg or 180 U/kg for a 25 g mouse administered intravenously weekly either from birth or beginning at 8 weeks of age surprisingly well tolerate the treatment and neither anaphylaxis nor antibody formation is observed. In mice treated from birth, survival increases from 236 to 271 days and the onset of motor deterioration is similarly delayed. In mice treated beginning at 8 weeks, no increases in survival or motor performance are seen. Outside the central nervous system, substantial clearance of autofluorescent storage material in many tissues is observed. Macrophages in spleen, liver and intestine are especially markedly improved, as are acinar cells of the pancreas and tubular cells of the kidney
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cho, S.; Dawson, G.
Enzymatic and molecular biological analysis of palmitoyl protein thioesterase deficiency in infantile neuronal ceroid lipofuscinosis
J. Neurochem.
71
323-329
1998
Homo sapiens
brenda
Hellsten, E.; Vesa, J.; Olkkonen, V.M.; Jalanko, A.; Peltonen, L.
Human palmitoyl protein thioesterase: evidence for lysosomal targeting of the enzyme and disturbed cellular routing in infantile neuronal ceroid lipofuscinosis
EMBO J.
15
5240-5245
1996
Homo sapiens
brenda
Vesa, J.; Hellsten, E.; Verkruyse, L.A.; Camp, L.A.; Rapola, J.; Santavuori, P.; Hofmann, S.L.; Peltonen, L.
Mutations in the palmitoyl protein thioesterase gene causing infantile neuronal ceroid lipofuscinosis
Nature
376
584-587
1995
Homo sapiens
brenda
Schriner, J.E.; Yi, W.; Hofmann, S.L.
cDNA and genomic cloning of human palmitoyl-protein thioesterase (PPT), the enzyme defective in infantile neuronal ceroid lipofuscinosis
Genomics
34
317-4322
1996
Homo sapiens (P50897), Homo sapiens
brenda
Verkruyse, L.A.; Hofmann, S.L.
Lysosomal targeting of palmitoyl-protein thioesterase
J. Biol. Chem.
271
15831-15836
1996
Homo sapiens
brenda
Camp, L.A.; Hofmann, S.L.
Assay and isolation of palmitoyl-protein thioesterase from bovine brain using palmitoylated H-Ras as substrate
Methods Enzymol.
250
336-347
1995
Bos taurus
brenda
Camp, L.A.; Hofmann, S.L.
Purification and properties of a palmitoyl-protein thioesterase that cleaves palmitate from H-Ras
J. Biol. Chem.
268
22566-22574
1993
Bos taurus
brenda
Slea, D.E.; Sohar, I.; Lackland, H.; Majercak, J.; Lobel, P.
Rat brain contains high levels of mannose-6-phosphorylated glycoproteins including enzymes and palmitoyl-protein thioesterase, an enzyme implicated in infantile neuronal lipofuscinosis
J. Biol. Chem.
271
19191-19198
1996
Rattus norvegicus
brenda
Lu, J.Y.; Verkruyse, L.A.; Hofmann, S.L.
Lipid thioesters derived from acylated proteins accumulate in infantile neuronal ceroid lipofuscinosis: correction of the defect in lymphoblasts by recombinant palmitoyl-protein thioesterase
Proc. Natl. Acad. Sci. USA
93
10046-10050
1996
Homo sapiens
brenda
Michel, J.B.; Michel, T.
The role of palmitoyl-protein thioesterase in the palmitoylation of endothelial nitric oxide synthetase
FEBS Lett.
405
356-362
1997
Bos taurus
brenda
Meng, L.; Sin, N.; Crews, C.M.
The antiproliferative agent didemnin B uncompetitively inhibits palmitoyl protein thioesterase
Biochemistry
37
10488-10492
1998
Homo sapiens
brenda
Lu, J.Y.; Verkruyse, L.A.; Hofmann, S.L.
The effects of lysosomotropic agents on normal and INCL cells provide further evidence for the lysosomal nature of palmitoyl-protein thioesterase function
Biochim. Biophys. Acta
1583
35-44
2002
Homo sapiens
brenda
Lukacs, Z.; Santavuori, P.; Keil, A.; Steinfeld, R.; Kohlschutter, A.
Rapid and simple assay for the determination of tripeptidyl peptidase and palmitoyl protein thioesterase activities in dried blood spots
Clin. Chem.
49
509-512
2003
Homo sapiens
brenda
Cho, S.K.; Hofmann, S.L.
pdf1, a palmitoyl protein thioesterase 1 ortholog in Schizosaccharomyces pombe: a yeast model of infantile Batten disease
Eukaryot. Cell
3
302-310
2004
Schizosaccharomyces pombe (O59747), Schizosaccharomyces pombe
brenda
Das, A.K.; Lu, J.Y.; Hofmann, S.L.
Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis
Hum. Mol. Genet.
10
1431-1439
2001
Homo sapiens
brenda
Lehtovirta, M.; Kyttala, A.; Eskelinen, E.L.; Hess, M.; Heinonen, O.; Jalanko, A.
Palmitoyl protein thioesterase (PPT) localizes into synaptosomes and synaptic vesicles in neurons: implications for infantile neuronal ceroid lipofuscinosis (INCL)
Hum. Mol. Genet.
10
69-75
2001
Homo sapiens, Mus musculus
brenda
Waliany, S.; Das, A.K.; Gaben, A.; Wisniewski, K.E.; Hofmann, S.L.
Identification of three novel mutations of the palmitoyl-protein thioesterase-1 (PPT1) gene in children with neuronal ceroid-lipofuscinosis
Hum. Mutat.
15
206-207
2000
Homo sapiens
brenda
Salonen, T.; Jarvela, I.; Peltonen, L.; Jalanko, A.
Detection of eight novel palmitoyl protein thioesterase (PPT) mutations underlying infantile neuronal ceroid lipofuscinosis (INCL;CLN1)
Hum. Mutat.
15
273-279
2000
Homo sapiens
brenda
Calero, G.; Gupta, P.; Nonato, M.C.; Tandel, S.; Biehl, E.R.; Hofmann, S.L.; Clardy, J.
The crystal structure of palmitoyl protein thioesterase-2 (PPT2) reveals the basis for divergent substrate specificities of the two lysosomal thioesterases, PPT1 and PPT2
J. Biol. Chem.
278
37957-37964
2003
Homo sapiens
brenda
Ahtiainen, L.; Van Diggelen, O.P.; Jalanko, A.; Kopra, O.
Palmitoyl protein thioesterase 1 is targeted to the axons in neurons
J. Comp. Neurol.
455
368-377
2003
Mus musculus
brenda
Salonen, T.; Heinonen-Kopra, O.; Vesa, J.; Jalanko, A.
Neuronal trafficking of palmitoyl protein thioesterase provides an excellent model to study the effects of different mutations which cause infantile neuronal ceroid lipofuscinocis
Mol. Cell. Neurosci.
18
131-140
2001
Homo sapiens
brenda
Suopanki, J.; Tyynela, J.; Baumann, M.; Haltia, M.
The expression of palmitoyl-protein thioesterase is developmentally regulated in neural tissues but not in nonneural tissues
Mol. Genet. Metab.
66
290-293
1999
Rattus norvegicus
brenda
Suopanki, J.; Lintunen, M.; Lahtinen, H.; Haltia, M.; Panula, P.; Baumann, M.; Tyynela, J.
Status epilepticus induces changes in the expression and localization of endogenous palmitoyl-protein thioesterase 1
Neurobiol. Dis.
10
247-257
2002
Rattus norvegicus
brenda
Suopanki, J.; Tyynela, J.; Baumann, M.; Haltia, M.
Palmitoyl-protein thioesterase, an enzyme implicated in neurodegeneration, is localized in neurons and is developmentally regulated in rat brain
Neurosci. Lett.
265
53-56
1999
Rattus norvegicus
brenda
Bellizzi, J.J., 3rd; Widom, J.; Kemp, C.; Lu, J.Y.; Das, A.K.; Hofmann, S.L.; Clardy, J.
The crystal structure of palmitoyl protein thioesterase 1 and the molecular basis of infantile neuronal ceroid lipofuscinosis
Proc. Natl. Acad. Sci. USA
97
4573-4578
2000
Homo sapiens
brenda
Kohan, R.; Noher de Halac, I.; Anzolini, V.T.; Cismondi, A.; Oller Ramirez, A.M.; Capra, A.P.; Dodelson de Kremer, R.
Palmitoyl protein thioesterase 1 (PPT1) and tripeptidyl peptidase-I (TPP-I) are expressed in the human saliva. A reliable and non-invasive source for the diagnosis of infantile (CLN1) and late infantile (CLN2) neuronal ceroid lipofuscinoses
Clin. Biochem.
38
492-494
2005
Homo sapiens
brenda
Zhang, Z.; Lee, Y.C.; Kim, S.J.; Choi, M.S.; Tsai, P.C.; Xu, Y.; Xiao, Y.J.; Zhang, P.; Heffer, A.; Mukherjee, A.B.
Palmitoyl-protein thioesterase-1 deficiency mediates the activation of the unfolded protein response and neuronal apoptosis in INCL
Hum. Mol. Genet.
15
337-346
2005
Mus musculus
brenda
Porter, M.Y.; Turmaine, M.; Mole, S.E.
Identification and characterization of Caenorhabditis elegans palmitoyl protein thioesterase 1
J. Neurosci. Res.
79
836-848
2005
Caenorhabditis elegans
brenda
Lyly, A.; von Schantz, C.; Salonen, T.; Kopra, O.; Saarela, J.; Jauhiainen, M.; Kyttaelae, A.; Jalanko, A.
Glycosylation, transport, and complex formation of palmitoyl protein thioesterase 1 (PPT1) - distinct characteristics in neurons
BMC Cell Biol.
8
22
2007
Homo sapiens (P50897)
brenda
Buff, H.; Smith, A.C.; Korey, C.A.
Genetic modifiers of Drosophila palmitoyl-protein thioesterase 1-induced degeneration
Genetics
176
209-220
2007
Drosophila sp. (in: flies)
brenda
Bannan, B.A.; Van Etten, J.; Kohler, J.A.; Tsoi, Y.; Hansen, N.M.; Sigmon, S.; Fowler, E.; Buff, H.; Williams, T.S.; Ault, J.G.; Glaser, R.L.; Korey, C.A.
The Drosophila protein palmitoylome: Characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases
Fly
2
198-214
2008
Drosophila melanogaster
brenda
Kim, S.J.; Zhang, Z.; Sarkar, C.; Tsai, P.C.; Lee, Y.C.; Dye, L.; Mukherjee, A.B.
Palmitoyl protein thioesterase-1 deficiency impairs synaptic vesicle recycling at nerve terminals, contributing to neuropathology in humans and mice
J. Clin. Invest.
118
3075-3086
2008
Homo sapiens, Mus musculus
brenda
Hirano, T.; Kishi, M.; Sugimoto, H.; Taguchi, R.; Obinata, H.; Ohshima, N.; Tatei, K.; Izumi, T.
Thioesterase activity and subcellular localization of acylprotein thioesterase 1/lysophospholipase 1
Biochim. Biophys. Acta
1791
797-805
2009
Homo sapiens (O75608), Homo sapiens
brenda
Tardy, C.; Sabourdy, F.; Garcia, V.; Jalanko, A.; Therville, N.; Levade, T.; Andrieu-Abadie, N.
Palmitoyl protein thioesterase 1 modulates tumor necrosis factor alpha-induced apoptosis
Biochim. Biophys. Acta
1793
1250-1258
2009
Mus musculus, Homo sapiens (P50897), Homo sapiens
brenda
Takano, K.; Shimono, M.; Shiota, N.; Kato, A.; Tomioka, S.; Oka, A.; Ohno, K.; Sathou, H.
Infantile neuronal ceroid lipofuscinosis: The first reported case in Japan diagnosed by palmitoyl-protein thioesterase enzyme activity deficiency
Brain Dev.
30
370-373
2008
Homo sapiens
brenda
Macauley, S.L.; Wozniak, D.F.; Kielar, C.; Tan, Y.; Cooper, J.D.; Sands, M.S.
Cerebellar pathology and motor deficits in the palmitoyl protein thioesterase 1-deficient mouse
Exp. Neurol.
217
124-135
2009
Mus musculus
brenda
Lu, J.Y.; Hu, J.; Hofmann, S.L.
Human recombinant palmitoyl-protein thioesterase-1 (PPT1) for preclinical evaluation of enzyme replacement therapy for infantile neuronal ceroid lipofuscinosis
Mol. Genet. Metab.
99
374-378
2010
Homo sapiens
brenda
Saja, S.; Buff, H.; Smith, A.C.; Williams, T.S.; Korey, C.A.
Identifying cellular pathways modulated by Drosophila palmitoyl-protein thioesterase 1 function
Neurobiol. Dis.
40
135-145
2010
Drosophila melanogaster, Drosophila sp. (in: flies)
brenda
Sanders, D.N.; Farias, F.H.; Johnson, G.S.; Chiang, V.; Cook, J.R.; OBrien, D.P.; Hofmann, S.L.; Lu, J.Y.; Katz, M.L.
A mutation in canine PPT1 causes early onset neuronal ceroid lipofuscinosis in a Dachshund
Mol. Genet. Metab.
100
349-356
2010
Canis lupus familiaris (Q5JZR0), Canis lupus familiaris
brenda
Chu-LaGraff, Q.; Blanchette, C.; OHern, P.; Denefrio, C.
The Batten disease Palmitoyl Protein Thioesterase 1 gene regulates neural specification and axon connectivity during Drosophila embryonic development
PLoS ONE
5
e14402
2010
Drosophila melanogaster
brenda
Aby, E.; Gumps, K.; Roth, A.; Sigmon, S.; Jenkins, S.E.; Kim, J.J.; Kramer, N.J.; Parfitt, K.D.; Korey, C.A.
Mutations in palmitoyl-protein thioesterase 1 alter exocytosis and endocytosis at synapses in Drosophila larvae
Fly
7
267-279
2014
Drosophila melanogaster (Q9W3C7), Drosophila melanogaster
brenda
Hu, J.; Lu, J.Y.; Wong, A.M.; Hynan, L.S.; Birnbaum, S.G.; Yilmaz, D.S.; Streit, B.M.; Lenartowicz, E.M.; Thompson, T.C.; Cooper, J.D.; Hofmann, S.L.
Intravenous high-dose enzyme replacement therapy with recombinant palmitoyl-protein thioesterase reduces visceral lysosomal storage and modestly prolongs survival in a preclinical mouse model of infantile neuronal ceroid lipofuscinosis
Mol. Genet. Metab.
107
213-221
2012
Mus musculus
brenda
Liu, Y.; Zhao, W.; Gu, G.; Lu, L.; Feng, J.; Guo, Q.; Ding, Z.
Palmitoyl-protein thioesterase 1 (PPT1): an obesity-induced rat testicular marker of reduced fertility
Mol. Reprod. Dev.
81
55-65
2014
Rattus norvegicus (P45479)
brenda
Spinelli, M.; Fusco, S.; Grassi, C.
Nutrient-dependent changes of protein palmitoylation Impact on nuclear enzymes and regulation of gene expression
Int. J. Mol. Sci.
19
E3820
2018
Homo sapiens
-
brenda
Scifo, E.; Szwajda, A.; Soliymani, R.; Pezzini, F.; Bianchi, M.; Dapkunas, A.; Debski, J.; Uusi-Rauva, K.; Dadlez, M.; Gingras, A.C.; Tyynelae, J.; Simonati, A.; Jalanko, A.; Baumann, M.H.; Lalowski, M.
Proteomic analysis of the palmitoyl protein thioesterase 1 interactome in SH-SY5Y human neuroblastoma cells
J. Proteomics
123
42-53
2015
Homo sapiens (P50897), Homo sapiens
brenda
Shyng, C.; Macauley, S.L.; Dearborn, J.T.; Sands, M.S.
Widespread expression of a membrane-tethered version of the soluble lysosomal enzyme palmitoyl protein thioesterase-1
JIMD Rep.
36
85-92
2017
Homo sapiens
brenda
Meyer, M.; Kovacs, A.D.; Pearce, D.A.
Decreased sensitivity of palmitoyl protein thioesterase 1-deficient neurons to chemical anoxia
Metab. Brain Dis.
32
275-279
2017
Mus musculus (Q88531)
brenda
Dearborn, J.T.; Ramachandran, S.; Shyng, C.; Lu, J.Y.; Thornton, J.; Hofmann, S.L.; Sands, M.S.
Histochemical localization of palmitoyl protein thioesterase-1 activity
Mol. Genet. Metab.
117
210-216
2016
Mus musculus
brenda
Segal-Salto, M.; Sapir, T.; Reiner, O.
Reversible cysteine acylation regulates the activity of human Palmitoyl-Protein Thioesterase 1 (PPT1)
PLoS ONE
11
e0146466
2016
Homo sapiens (P50897), Homo sapiens
brenda
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EXTERNAL LINKS (specific for EC-Number 3.1.2.22)
Transporter Classification Database (TCDB): 4.C.3.2.1, 8.A.161.1.1
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Release 2023.1 (January 2023)
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