Literature summary for 2.3.1.225 extracted from

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

Search for more literature for 2.3.1.225

Activating Compound

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

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
additional information	Drosophila melanogaster	in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
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
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
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
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
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
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
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
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
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
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
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
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
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
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

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview	Drosophila melanogaster	?	-	?
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	?	-	?
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	?	-	?
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	?	-	?
additional information	APT1 has acyl-CoA hydrolase activity	Rattus norvegicus	?	-	?
additional information	APT1 has acyl-CoA hydrolase activity	Saccharomyces cerevisiae	?	-	?
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
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
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
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
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
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
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
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
palmitoyl-CoA + [protein]-L-cysteine	-	Drosophila melanogaster	[protein]-S-palmitoyl-L-cysteine + CoA	-	r
palmitoyl-CoA + [protein]-L-cysteine	-	Homo sapiens	[protein]-S-palmitoyl-L-cysteine + CoA	-	r
palmitoyl-CoA + [protein]-L-cysteine	-	Rattus norvegicus	[protein]-S-palmitoyl-L-cysteine + CoA	-	r
palmitoyl-CoA + [protein]-L-cysteine	-	Saccharomyces cerevisiae	[protein]-S-palmitoyl-L-cysteine + CoA	-	r
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
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
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
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
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
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
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
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
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
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

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

Synonyms

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

General Information

General Information	Comment	Organism
malfunction	apt1 null cells exhibit almost no acylprotein thioesterase activity toward palmitoyl-Gialpha1	Saccharomyces cerevisiae
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
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
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
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
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
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
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
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