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Information on EC 3.1.2.22 - palmitoyl[protein] hydrolase and Organism(s) Schizosaccharomyces pombe and UniProt Accession O59747
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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
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ceroid
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infantile
- lipofuscinosis
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palmitoylated
- lysosomal
- neurodegenerative
- batten
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depalmitoylation
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ppt1-deficient
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autofluorescent
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grods
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tripeptidyl
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osmiophilic
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s-acylated
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late-infantile
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lincl
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thioesterases
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lipid-modified
- ceroid-lipofuscinosis
- medicine
- nutrition
The taxonomic range for the selected organisms is: Schizosaccharomyces pombe
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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-thioesterase, palmitoyl protein thioesterase-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acyl protein thioester hydrolase
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G14
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GenBank AF020543-derived protein GI 2501961
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GenBank L42809-derived protein GI 1160967
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Hydrolase, acyl protein thioester
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Hydrolase, acyl protein thioester (cattle clone pBovPPT-18 precursor reduced)
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Hydrolase, acyl protein thioester (cattle pBovPPT-25 precursor reduced)
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Hydrolase, acyl protein thioester (human clone B lysosome-associated isoenzyme 2)
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Hydrolase, acyl protein thioester (human clone pHuPPT-5')
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Hydrolase, acyl protein thioester (ox clone pBovPPT-18 precursor reduced)
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Hydrolase, acyl protein thioester (ox pBovPPT-25 precursor reduced)
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Hydrolase, acyl protein thioester (rat clone pRatPPT-44 precursor reduced)
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Palmitoyl-protein thioesterase
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Palmitoyl-protein thioesterase (bovine clone pBovPPT-17 precursor)
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Palmitoyl-protein thioesterase (bovine clone pBovPPT-25 precursor)
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Palmitoyl-protein thioesterase (human clone pHuPPT-5')
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Palmitoyl-protein thioesterase (rat clone pRatPPT-44 precursor)
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Palmitoyl-protein thioesterase PPT2 (human clone B lysosome associated)
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PPT
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PPT1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl[protein] + H2O = palmitate + protein
specific for long-chain thioesters of fatty acids from S-acylated residues in proteins, palmitoyl cysteine and palmitoyl-CoA
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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.
CAS REGISTRY NUMBER
COMMENTARY
150605-49-5
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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)
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
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
artificial substrate
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?
additional information
?
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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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?
additional information
?
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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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?
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
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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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 31000, processed enzyme, SDS-PAGE, x * 101000, unprocessed enzyme, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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