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Information on EC 2.3.1.225 - protein S-acyltransferase
for references in articles please use BRENDA:EC2.3.1.225
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.225 protein S-acyltransferase
IUBMB Comments
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
The enzyme appears in viruses and cellular organisms
- 2.3.1.225
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palmitoylation
- palmitate
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s-acylation
- huntingtin
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palmitoylation-dependent
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huntingtin-interacting
- 2-bromopalmitate
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s-acyltransferases
- medicine
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autoacylation
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16-carbon
- snap25
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acyl-acyl
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palmitoylation-deficient
Reaction Schemes
showSynonyms
hip14, dhhc3, palmitoyl acyltransferase, dhhc5, zdhhc5, dhhc2, akr1p, zdhhc3, protein acyltransferase, dhhc protein, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Akr1
APT1
DHHC protein
DHHC protein acyltransferase
DHHC-CRD S-acyltransferase
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58
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DHHC2
DHHC3
DHHC5
Erf2
palmitoyl acyltransferase
Pat
Pfa3
Pfa4
PFA5
protein acyl transferase
protein acyltransferase
SEC18p
Swf1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
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palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
two-step transfer mechanism, ping-pong kinetic mechanism
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palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA
two-step transfer mechanism, ping-pong kinetic mechanism
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SYSTEMATIC NAME
IUBMB Comments
palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
The enzyme catalyses the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + [Gialpha1]-L-cysteine
[protein]-S-myristoyl-L-cysteine + CoA
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Substrates: GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Chs3]-L-cysteine
[Chs3]-S-palmitoyl-L-cysteine + CoA
Substrates: -
Products: -
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palmitoyl-CoA + [endothelial nitric oxide synthase]-L-cysteine
[endothelial nitric oxide synthase]-S-palmitoyl-L-cysteine + CoA
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Substrates: isozyme DHHC-21
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palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [G-protein alpha subunit Galphai]-L-cysteine
[G-protein alpha subunit Galphai]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [Ga protein]-L-cysteine
[Ga protein]-S-palmitoyl-L-cysteine + CoA
Substrates: substrate of DHHC3 and DHHC7
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palmitoyl-CoA + [GAD65]-L-cysteine
[GAD65]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [GAP-43 protein]-L-cysteine
[GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: substrate of DHHC7 and DHHC15
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palmitoyl-CoA + [GOalpha1]-L-cysteine
[GOalpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [GSalpha1]-L-cysteine
[GSalpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: Gsa is not a myristoylated protein, but is palmitoylated at Cys3
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palmitoyl-CoA + [htt(1-548)]-L-cysteine
[htt(1-548)]-S-palmitoyl-L-cysteine + CoA
Substrates: N-terminal fragment of htt(1-548)
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palmitoyl-CoA + [Lck]-L-cysteine
[Lck]-S-palmitoyl-L-cysteine + CoA
Substrates: nonreceptor tyrosine kinase
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palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Pat10]-L-cysteine
[PAT10]-S-palmitoyl-L-cysteine + CoA
Substrates: -
Products: autoacylation
Products: autoacylation
?
palmitoyl-CoA + [PAT14]-L-cysteine
[PAT14]-S-palmitoyl-L-cysteine + CoA
Substrates: -
Products: autoacylation
Products: autoacylation
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palmitoyl-CoA + [Pfa4]-L-cysteine
[Pfa4]-S-palmitoyl-L-cysteine + CoA
Substrates: autoacylation
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palmitoyl-CoA + [phospholemman]-L-cysteine
[phospholemman]-S-palmitoyl-L-cysteine + CoA
Substrates: -
Products: isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. C40 is the principal palmitoylation site
Products: isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. C40 is the principal palmitoylation site
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palmitoyl-CoA + [PSD-95]-L-cysteine
[PSD-95]-S-palmitoyl-L-cysteine + CoA
Substrates: low activity
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palmitoyl-CoA + [Ras1p]-L-cysteine
[Ras1p]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [Rho2 protein]-L-cysteine
[Rho2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Rho3 protein]-L-cysteine
[Rho3 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
palmitoyl-CoA + [Ste18 protein]-L-cysteine
[Ste18 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Swf1]-L-cysteine
[Swf1]-S-palmitoyl-L-cysteine + CoA
Substrates: autoacylation
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palmitoyl-CoA + [synaptotagmin I ]-L-cysteine
[synaptotagmin I ]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Yck2 protein]-L-cysteine
[Yck2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
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Substrates: yeast casein kinase Yck2 is a substrate of Akr1
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palmitoyl-CoA + [Yck3 protein]-L-cysteine
[Yck3 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ycp4 protein]-L-cysteine
[Ycp4 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ykl047w protein]-L-cysteine
[Ykl047w protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ypl199c protein]-L-cysteine
[Ypl199c protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ypl236c protein]-L-cysteine
[Ypl236c protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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stearoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-stearoyl-L-cysteine + CoA
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Substrates: Rhodopsin containing rod outer segment membranes prepared from fresh, dark-adapted bovine retinae
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palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: purified recombinant Gialpha1
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palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: purified recombinant Gialpha1
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: recombinant myristoylated G protein alpha subunit and bovine brain betagamma subunits. G-protein substrate specificity of PAT activity, overview. wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: G protein alpha subunit, wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S, myristoylated or not myristoylated
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
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palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
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Substrates: GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
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palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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Substrates: H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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Substrates: H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
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Substrates: H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
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palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
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Substrates: peptide substrate si tagged via ethylenediamine with fluorescent NBD
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palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
Substrates: peptide substrate si tagged via ethylenediamine with fluorescent NBD
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palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
B3DN87, O80685, Q0WQK2, Q3EBC2, Q3EC11, Q500Z2, Q52T38, Q5M757, Q6DR03, Q7XA86, Q8L5Y5, Q8VYP5, Q8VYS8, Q93VV0, Q94C49, Q9C533, Q9FLM3, Q9LIE4, Q9LIH7, Q9M115, Q9M1K5, Q9M306, Q9SB58
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: PAT10-mediated palmitoylation is critical for vacuolar function by regulating membrane association or the activities of tonoplast proteins
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
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Substrates: -
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palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
Substrates: possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7
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palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
Substrates: by Ras PAT containing the DHHC9 protein subunit
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palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
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Substrates: yeast Ras protein is a substrate of Erf2
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
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Substrates: 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
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palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
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Substrates: PAT incorporates fatty acid into rhodopsin with higher efficiency, 10times higher initial rate, as compared to autoacylation, presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT
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palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
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Substrates: PAT incorporates fatty acid into rhodopsin with higher efficiency, 10times higher initial rate, as compared to autoacylation, presence of deacylated, free cysteine residues in dark-adapted rhodopsin increases palmitoylation via PAT. Rhodopsin containing rod outer segment membranes prepared from fresh, dark-adapted bovine retinae
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palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
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Substrates: minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
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palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
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Substrates: minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
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palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
Substrates: substrate of DHHC3 and DHHC7
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palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
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Substrates: yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
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Substrates: yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
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Substrates: yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
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palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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Substrates: recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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Substrates: recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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Substrates: recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modi¢cation
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palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
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Substrates: recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
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palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
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Substrates: Vac8 is a substrate of Pfa3, Vac8 is a myristoylated and palmitoylated protein that localizes to the vacuolar membrane and is required for vacuolar fusion
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palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
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Substrates: Vac8 is a substrate of Pfa3 performing S-palmitoylation of up to three N-terminal cysteines, Vac8 is N-myristoylated at an N-terminal glycine residue. Vac8 is not palmitoylated by Akr1, Erf2/Erf4, Pfa4, or Pfa5 in vitro
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palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
Substrates: -
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additional information
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Substrates: Kinetics and substrate specificity of PAT, overview
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additional information
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Substrates: PAT activity displays specificity for the acyl donor, efficiently utilizing long-chain acyl-CoAs, but not free fatty acid or S-palmitoyl-N-acetylcysteamine. PAT also shows thiolase activity
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additional information
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Substrates: PAT fatty acyl-CoA chain length specificity in vitro, overview. PAT shows G-protein substrate specificity of PAT activity, overview. Mutation of the prenylated cysteine residue to serine, C68S, in the gamma2 subunit yields a nonprenylated gamma that heterodimerizes with the beta1 subunit. The mutant betagammaC68S binds to myristoylated rGialpha1, forming a heterotrimer that is acylated in vitro with efficiency similar to that of the wild-type heterotrimer
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additional information
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Substrates: PAT activity displays specificity for the acyl donor, efficiently utilizing long-chain acyl-CoAs, but not free fatty acid or S-palmitoyl-N-acetylcysteamine. PAT also shows thiolase activity
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additional information
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Substrates: in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview
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additional information
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Substrates: 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
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additional information
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Substrates: complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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Substrates: complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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Substrates: complexity of HIP14's substrate specificity, in vitro, HIP14 has PAT activity for the N-terminal fragment of htt(1-548), SNAP-25, PSD-95, GAD65, and synaptotagmin I but not for synaptotagmin VII and paralemmin
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additional information
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Substrates: DHHC2 has a broad protein substrate specificity. DHHC2 transfers fatty acids from all acyl-CoA chain lengths tested, consistent with it having a broad specificity for long chain acyl-CoAs, and acyl-CoAs of 14 carbons and longer inhibit palmitoyl-CoA labeling of both substrate and enzyme. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
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additional information
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Substrates: DHHC3 has a broad protein substrate specificity, but only myristoyl-, palmitoyl-, and palmioleoyl-CoA are effective, and longer acyl-CoAs compete less well. The acyl-CoA chain length specificity of DHHC enzyme autoacylation parallels substrate specificity, overview
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additional information
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Substrates: 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
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additional information
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Substrates: APT1 has acyl-CoA hydrolase activity
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additional information
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Substrates: G-protein substrate specificity of PAT activity, overview. Mutation of the prenylated cysteine residue to serine, C68S, in the gamma2 subunit yields a nonprenylated gamma that heterodimerizes with the beta1 subunit. The mutant betagammaC68S binds to myristoylated rGialpha1, forming a heterotrimer that is acylated in vitro with efficiency similar to that of the wild-type heterotrimer
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additional information
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Substrates: 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
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additional information
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Substrates: APT1 has acyl-CoA hydrolase activity
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additional information
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Substrates: PATis speci¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
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additional information
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Substrates: PATis speci¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
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