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Literature summary extracted from

  • 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 (2000), Proc. Natl. Acad. Sci. USA, 97, 4573-4578.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.2.22 expression of wild-type and mutant in COS-1 cells Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.2.22 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 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.2.22 D233N site-directed mutagenesis, inactive mutant Homo sapiens
3.1.2.22 D79G site-directed mutagenesis, highly reduced activity Homo sapiens
3.1.2.22 H289A site-directed mutagenesis, inactive mutant Homo sapiens
3.1.2.22 N197Q site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity Homo sapiens
3.1.2.22 N197Q/N212Q site-directed mutagenesis, mutation of glycosylation sites, slightly reduced activity, mutant shows 10% of the wild-type expression level Homo sapiens
3.1.2.22 N197Q/N212Q/N232Q site-directed mutagenesis, mutation of all glycosylation sites, inactive mutant Homo sapiens
3.1.2.22 N197Q/N232Q site-directed mutagenesis, mutation of glycosylation sites, reduced activity Homo sapiens
3.1.2.22 N212Q site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity Homo sapiens
3.1.2.22 N212Q/N232Q site-directed mutagenesis, mutation of glycosylation sites, highly reduced activity Homo sapiens
3.1.2.22 N232Q site-directed mutagenesis, mutation of a glycosylation site, slightly reduced activity Homo sapiens
3.1.2.22 S115A site-directed mutagenesis, inactive mutant Homo sapiens
3.1.2.22 T75P site-directed mutagenesis, highly reduced activity Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.2.22 lysosome
-
 Homo sapiens 5764
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.22 additional information Homo sapiens enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, molecular basis ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.22 Homo sapiens
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.2.22 glycoprotein N-glycosylation at Asn232, Asn197, and Asn212, essential for activity Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.2.22 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 Homo sapiens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.22 additional information enzyme deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL, molecular basis Homo sapiens ?
-
 ?
3.1.2.22 palmitoyl-[protein] + H2O
-
 Homo sapiens palmitate + protein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.2.22 palmitoyl protein thioesterase
-
 Homo sapiens