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Literature summary extracted from

  • Linder, M. E.; Deschenes, R. J.
    New insights into the mechanisms of protein palmitoylation (2003), Biochemistry, 42, 4311-4320.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.3.1.225 ATP both intermediate formation and acyl transfer to Yck2p by Akr1p are stimulated by ATP Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.225 cytosol enzyme class II Drosophila melanogaster 5829
-
2.3.1.225 cytosol enzyme class II Homo sapiens 5829
-
2.3.1.225 cytosol enzyme class II Rattus norvegicus 5829
-
2.3.1.225 cytosol enzyme class II Saccharomyces cerevisiae 5829
-
2.3.1.225 endoplasmic reticulum
-
 Drosophila melanogaster 5783
-
2.3.1.225 endoplasmic reticulum
-
 Homo sapiens 5783
-
2.3.1.225 endoplasmic reticulum
-
 Rattus norvegicus 5783
-
2.3.1.225 endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-
2.3.1.225 Golgi membrane
-
 Drosophila melanogaster 139
-
2.3.1.225 Golgi membrane
-
 Homo sapiens 139
-
2.3.1.225 Golgi membrane
-
 Rattus norvegicus 139
-
2.3.1.225 Golgi membrane
-
 Saccharomyces cerevisiae 139
-
2.3.1.225 lysosome enzyme class I Drosophila melanogaster 5764
-
2.3.1.225 lysosome enzyme class I Homo sapiens 5764
-
2.3.1.225 lysosome enzyme class I Rattus norvegicus 5764
-
2.3.1.225 lysosome enzyme class I Saccharomyces cerevisiae 5764
-
2.3.1.225 plasma membrane
-
 Drosophila melanogaster 5886
-
2.3.1.225 plasma membrane
-
 Homo sapiens 5886
-
2.3.1.225 plasma membrane
-
 Rattus norvegicus 5886
-
2.3.1.225 plasma membrane
-
 Saccharomyces cerevisiae 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.225 additional information Drosophila melanogaster in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview ?
-
 ?
2.3.1.225 additional information Rattus norvegicus in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA ?
-
 ?
2.3.1.225 additional information Saccharomyces cerevisiae in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA ?
-
 ?
2.3.1.225 additional information Homo sapiens in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. G protein alpha subunit GsR is first acylated at Cys-3, then the palmitate is transferred to the amino group of Gly-2 through a cyclic intermediate as is postulated for hedgehog ?
-
 ?
2.3.1.225 myristoyl-CoA + [Gialpha1]-L-cysteine Rattus norvegicus GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1 [protein]-S-myristoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine Saccharomyces cerevisiae Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1 [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine Rattus norvegicus GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1 [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [H-Ras]-L-cysteine Rattus norvegicus H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1 [H-Ras]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [H-Ras]-L-cysteine Saccharomyces cerevisiae H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1 [H-Ras]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Drosophila melanogaster S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Homo sapiens S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Rattus norvegicus S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Saccharomyces cerevisiae S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Ras1p]-L-cysteine Saccharomyces cerevisiae Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein [Ras1p]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Ras2p]-L-cysteine Saccharomyces cerevisiae Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein. both Erf2p and Erf4p are involved in the palmitoylation of Ras2p, overview. Mutation of the palmitoylated Cys to Ser abolishes palmitoylation and results in a mislocalization of Ras2p from the plasma membrane to endomembranes. Yeast Erf2p-Erf4p Ras PAT work best with yeast Ras2 protein and less well with mammalian myristoylated GiR subunits or mammalian Ha-Ras. Long chain acyl-CoA substrates, 16 and 18 carbons, are preferred over shorter acyl chains, below 14 carbons [Ras2p]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [RGS4]-L-cysteine Rattus norvegicus RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1 [RGS4]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [RGS4]-L-cysteine Saccharomyces cerevisiae RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1 [RGS4]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Yck2p]-L-cysteine Saccharomyces cerevisiae Akr1p is a palmitoyltransferase for Yck2p that catalyzes the transfer of palmitate from palmitoyl-CoA to a C-terminal Cys residue, formation of an Akr1p-palmitoyl intermediate [Yck2p]-S-palmitoyl-L-cysteine + CoA
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.225 Drosophila melanogaster
-
-
-
2.3.1.225 Homo sapiens
-
-
-
2.3.1.225 Rattus norvegicus
-
-
-
2.3.1.225 Saccharomyces cerevisiae
-
 genes ERF2 and AKR1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.225 Akr1p is purified from yeast to apparent homogeneity Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.225 additional information in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview Drosophila melanogaster ?
-
 ?
2.3.1.225 additional information in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA Rattus norvegicus ?
-
 ?
2.3.1.225 additional information in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. Effects of APT1 on palmitate turnover on Gsalpha are not due to effects on the rate of turnover of palmitoyl-CoA Saccharomyces cerevisiae ?
-
 ?
2.3.1.225 additional information in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview. G protein alpha subunit GsR is first acylated at Cys-3, then the palmitate is transferred to the amino group of Gly-2 through a cyclic intermediate as is postulated for hedgehog Homo sapiens ?
-
 ?
2.3.1.225 additional information APT1 has acyl-CoA hydrolase activity Rattus norvegicus ?
-
 ?
2.3.1.225 additional information APT1 has acyl-CoA hydrolase activity Saccharomyces cerevisiae ?
-
 ?
2.3.1.225 myristoyl-CoA + [Gialpha1]-L-cysteine GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1 Rattus norvegicus [protein]-S-myristoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1 Saccharomyces cerevisiae [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1 Rattus norvegicus [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1 Saccharomyces cerevisiae [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1 Rattus norvegicus [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [H-Ras]-L-cysteine H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1 Rattus norvegicus [H-Ras]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [H-Ras]-L-cysteine H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1 Rattus norvegicus [H-Ras]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [H-Ras]-L-cysteine H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1 Saccharomyces cerevisiae [H-Ras]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Drosophila melanogaster [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Homo sapiens [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Rattus norvegicus [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Saccharomyces cerevisiae [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins Drosophila melanogaster [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins Homo sapiens [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins Rattus norvegicus [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine S-palmitoylation is the reversible addition of palmitate or other long chain fatty acids to proteins at cysteine residues via a thioester linkage. The types of proteins that undergo palmitoylation are quite diverse and include intrinsic and peripherally associated membrane proteins, as well as mitochondrial proteins Saccharomyces cerevisiae [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Ras1p]-L-cysteine Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein Saccharomyces cerevisiae [Ras1p]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Ras2p]-L-cysteine Ras oncogene homologues, Ras1p and Ras2p, undergo reversible palmitoylation by Erf2p on a Cys residue adjacent to the canonical CaaX box prenylation motif at the C-terminus of the protein. both Erf2p and Erf4p are involved in the palmitoylation of Ras2p, overview. Mutation of the palmitoylated Cys to Ser abolishes palmitoylation and results in a mislocalization of Ras2p from the plasma membrane to endomembranes. Yeast Erf2p-Erf4p Ras PAT work best with yeast Ras2 protein and less well with mammalian myristoylated GiR subunits or mammalian Ha-Ras. Long chain acyl-CoA substrates, 16 and 18 carbons, are preferred over shorter acyl chains, below 14 carbons Saccharomyces cerevisiae [Ras2p]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [RGS4]-L-cysteine RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1 Rattus norvegicus [RGS4]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [RGS4]-L-cysteine RGS4 is palmitoylated at two cysteine residues near its amino terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1 Saccharomyces cerevisiae [RGS4]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [RGS4]-L-cysteine RGS4 is palmitoylated at two cysteine residues near its N-terminus (C2 and C12) and a cysteine residue in the RGS core domain, substrate of APT1 Rattus norvegicus [RGS4]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Yck2p]-L-cysteine Akr1p is a palmitoyltransferase for Yck2p that catalyzes the transfer of palmitate from palmitoyl-CoA to a C-terminal Cys residue, formation of an Akr1p-palmitoyl intermediate Saccharomyces cerevisiae [Yck2p]-S-palmitoyl-L-cysteine + CoA
-
 r

Subunits

EC Number Subunits Comment Organism
2.3.1.225 More yeast S-palmitoyltransferases contain DHHC-cysteine rich domains Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
2.3.1.225 Akr1p
-
 Saccharomyces cerevisiae
2.3.1.225 APT1
-
 Rattus norvegicus
2.3.1.225 APT1
-
 Saccharomyces cerevisiae
2.3.1.225 Erf2p
-
 Saccharomyces cerevisiae
2.3.1.225 Pat
-
 Drosophila melanogaster
2.3.1.225 Pat
-
 Homo sapiens
2.3.1.225 Pat
-
 Rattus norvegicus
2.3.1.225 Pat
-
 Saccharomyces cerevisiae
2.3.1.225 protein acyl transferase
-
 Drosophila melanogaster
2.3.1.225 protein acyl transferase
-
 Homo sapiens
2.3.1.225 protein acyl transferase
-
 Rattus norvegicus
2.3.1.225 protein acyl transferase
-
 Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
2.3.1.225 malfunction apt1 null cells exhibit almost no acylprotein thioesterase activity toward palmitoyl-Gialpha1 Saccharomyces cerevisiae
2.3.1.225 additional information one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization Drosophila melanogaster
2.3.1.225 additional information one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization Homo sapiens
2.3.1.225 additional information one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization Rattus norvegicus
2.3.1.225 additional information one enzyme family is lysosomal and is involved in protein degradation. The second is cytosolic and removes palmitoyl moieties preferentially from proteins associated with membranes. PAT activity requires detergent, e.g. Triton X-100, for solubilization Saccharomyces cerevisiae
2.3.1.225 physiological function reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association Drosophila melanogaster
2.3.1.225 physiological function reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association Homo sapiens
2.3.1.225 physiological function reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association Rattus norvegicus
2.3.1.225 physiological function reversible protein palmitoylation plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Mechanisms that underlie addition and removal of palmitate from proteins, detailed overview. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association Saccharomyces cerevisiae