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Literature summary for 3.1.2.22 extracted from

  • 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 (2003), J. Biol. Chem., 278, 37957-37964.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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 Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information residues involved in ligand binding differ between PPT1 and PPT2, exchange by site-directed mutagenesis and functional analysis, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome PPT1 and PPT2 Homo sapiens 5764
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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2 lysosomal enzyme forms PPT1 and PPT2
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Purification (Commentary)

Purification (Comment) Organism
recombinant PPT2 from overexpressing insect cells, recombinant PPT2 mutant from COS cells Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
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 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl 6-S-palmitoyl-6-thio-beta-D-glucoside + H2O
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Homo sapiens 4-methylumbelliferyl 6-thio-beta-D-glucoside + palmitate
-
?
additional information structural differences in the 2 enzyme fomrs PPT1 and PPT2, PPT2 does not hydrolyze substrates with bulky head groups Homo sapiens ?
-
?
additional information PPT1 deficiency causes progressive neurological disorder infantile neuronal ceroid lipofuscinosis, INCL Homo sapiens ?
-
?
palmitoyl-CoA + H2O preferred substrate of PPT2 Homo sapiens palmitate + CoA
-
?
S-palmitoyl-N-acetyl-O-carboxymethyl-cysteine + H2O enzyme form PPT1, not PPT2 Homo sapiens N-acetyl-O-carboxymethyl-cysteine + palmitate
-
?
S-palmitoyl-N-acetylcysteamine + H2O enzyme form PPT1, not PPT2 Homo sapiens N-acetylcysteamine + palmitate
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?

Synonyms

Synonyms Comment Organism
palmitoyl protein thioesterase-1
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Homo sapiens
palmitoyl protein thioesterase-2
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Homo sapiens
PPT1
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Homo sapiens
PPT2
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
assay at Homo sapiens