2.3.1.225: protein S-acyltransferase
This is an abbreviated version!
For detailed information about protein S-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.225
-
2.3.1.225
-
palmitoylation
-
palmitate
-
s-acylation
-
huntingtin
-
palmitoylation-dependent
-
huntingtin-interacting
-
2-bromopalmitate
-
s-acyltransferases
-
medicine
-
autoacylation
-
16-carbon
-
snap25
-
acyl-acyl
-
palmitoylation-deficient
- 2.3.1.225
-
palmitoylation
- palmitate
-
s-acylation
- huntingtin
-
palmitoylation-dependent
-
huntingtin-interacting
- 2-bromopalmitate
-
s-acyltransferases
- medicine
-
autoacylation
-
16-carbon
- snap25
-
acyl-acyl
-
palmitoylation-deficient
Reaction
Synonyms
Akr1, Akr1p, APT1, Asp-His-His-Cys motif palmitoyl transferase, At3g51390, DHHC palmitoyl transferase, DHHC protein, DHHC protein acyltransferase, DHHC-2, DHHC-21, DHHC-21 palmitoyl transferase, DHHC-3, DHHC-3 palmitoyl transferase, DHHC-7, DHHC-8, DHHC-CRD S-acyltransferase, DHHC16, DHHC17, DHHC2, DHHC3, DHHC4, DHHC5, Erf2, Erf2p, G-protein palmitoyltransferase, HIP14, palmitoyl acyltransferase, Pat, PAT10, PAT14, PAT15, PAT21, PAT24, PAT4, Pfa3, Pfa4, PFA5, protein acyl transferase, protein acyltransferase, protein S-acyl transferase 4, Ras PAT, S-protein acyltransferase, SEC18p, Swf1, ZDHHC3, ZDHHC5
ECTree
2.3.1.225 protein S-acyltransferaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 2.3.1.225 - protein S-acyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
myristoyl-CoA + [Gialpha1]-L-cysteine
[protein]-S-myristoyl-L-cysteine + CoA
-
GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
-
-
r
palmitoyl-CoA + [Chs3]-L-cysteine
[Chs3]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [endothelial nitric oxide synthase]-L-cysteine
[endothelial nitric oxide synthase]-S-palmitoyl-L-cysteine + CoA
-
isozyme DHHC-21
-
-
r
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
-
-
-
-
r
palmitoyl-CoA + [Ga protein]-L-cysteine
[Ga protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
-
-
r
palmitoyl-CoA + [GAD65]-L-cysteine
[GAD65]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [GAP-43 protein]-L-cysteine
[GAP-43 protein]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC7 and DHHC15
-
-
r
palmitoyl-CoA + [GOalpha1]-L-cysteine
[GOalpha1]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [GSalpha1]-L-cysteine
[GSalpha1]-S-palmitoyl-L-cysteine + CoA
-
Gsa is not a myristoylated protein, but is palmitoylated at Cys3
-
-
r
palmitoyl-CoA + [htt(1-548)]-L-cysteine
[htt(1-548)]-S-palmitoyl-L-cysteine + CoA
N-terminal fragment of htt(1-548)
-
-
r
palmitoyl-CoA + [Lck]-L-cysteine
[Lck]-S-palmitoyl-L-cysteine + CoA
nonreceptor tyrosine kinase
-
-
r
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
-
autoacylation
-
?
palmitoyl-CoA + [PAT14]-L-cysteine
[PAT14]-S-palmitoyl-L-cysteine + CoA
-
autoacylation
-
?
palmitoyl-CoA + [Pfa4]-L-cysteine
[Pfa4]-S-palmitoyl-L-cysteine + CoA
autoacylation
-
-
?
palmitoyl-CoA + [phospholemman]-L-cysteine
[phospholemman]-S-palmitoyl-L-cysteine + CoA
-
isoform DHHC5 palmitoylates cardiac phosphoprotein phospholemman at two juxtamembrane cysteines, C40 and C42. C40 is the principal palmitoylation site
-
?
palmitoyl-CoA + [PSD-95]-L-cysteine
[PSD-95]-S-palmitoyl-L-cysteine + CoA
low activity
-
-
r
palmitoyl-CoA + [Ras1p]-L-cysteine
[Ras1p]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Ras2p]-L-cysteine
[Ras2p]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Rho2 protein]-L-cysteine
[Rho2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Rho3 protein]-L-cysteine
[Rho3 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
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
-
-
-
?
palmitoyl-CoA + [Swf1]-L-cysteine
[Swf1]-S-palmitoyl-L-cysteine + CoA
autoacylation
-
-
?
palmitoyl-CoA + [synaptotagmin I ]-L-cysteine
[synaptotagmin I ]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [Yck2 protein]-L-cysteine
[Yck2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck2p]-L-cysteine
[Yck2p]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Yck2]-L-cysteine
[Yck2]-S-palmitoyl-L-cysteine + CoA
-
yeast casein kinase Yck2 is a substrate of Akr1
-
-
r
palmitoyl-CoA + [Yck3 protein]-L-cysteine
[Yck3 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ycp4 protein]-L-cysteine
[Ycp4 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ykl047w protein]-L-cysteine
[Ykl047w protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ypl199c protein]-L-cysteine
[Ypl199c protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ypl236c protein]-L-cysteine
[Ypl236c protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
stearoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-stearoyl-L-cysteine + CoA
-
Rhodopsin containing rod outer segment membranes prepared from fresh, dark-adapted bovine retinae
-
-
r
palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
purified recombinant Gialpha1
-
-
r
palmitoyl-CoA + [G protein alpha subunit Gialpha1]-L-cysteine
[G protein alpha subunit Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
purified recombinant Gialpha1
-
-
r
palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
GiR1 is myristoylated at its N-terminus and palmitoylated at an adjacent cysteine, substrate of APT1
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
G protein alpha subunit, wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S, myristoylated or not myristoylated
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
Gialpha1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, preferred substrate of APT1
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
GiR1 is myristoylated at its amino terminus and palmitoylated at an adjacent cysteine, substrate of APT1
-
-
r
palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gpa1 protein]-L-cysteine
[Gpa1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Gpa2 protein]-L-cysteine
[Gpa2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
-
H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
-
-
r
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
-
H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
-
-
r
palmitoyl-CoA + [H-Ras]-L-cysteine
[H-Ras]-S-palmitoyl-L-cysteine + CoA
-
H-Ras is palmitoylated at two cysteine residues immediately upstream of its farnesylated and carboxylmethylated C-terminus, substrate of APT1
-
-
r
palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Lcb4 protein]-L-cysteine
[Lcb4 prpotein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Meh1 protein]-L-cysteine
[Meh1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn1 protein]-L-cysteine
[Mnn1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn10 protein]-L-cysteine
[Mnn10 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Mnn11 protein]-L-cysteine
[Mnn11 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [N-myristoylated G-protein alphai1]-L-cysteine
[N-myristoylated G-protein alphai1]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
-
peptide substrate si tagged via ethylenediamine with fluorescent NBD
-
-
r
palmitoyl-CoA + [N-myristoylated Gly-Cys-Gly tripeptide]-L-cysteine
[N-myristoylated Gly-Cys-Gly tripeptide]-S-palmitoyl-L-cysteine + CoA
peptide substrate si tagged via ethylenediamine with fluorescent NBD
-
-
r
palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Pin2 protein]-L-cysteine
[Pin2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
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
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
PAT10-mediated palmitoylation is critical for vacuolar function by regulating membrane association or the activities of tonoplast proteins
-
-
?
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [PSD95]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
possible substrate of DHHC15 and, to a lesser extent, DHHC2, DHHC3, and DHHC7
-
-
r
palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Psr1 protein]-L-cysteine
[Psr1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras1 protein]-L-cysteine
[Ras1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras2 protein]-L-cysteine
[Ras2 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
by Ras PAT containing the DHHC9 protein subunit
-
-
r
palmitoyl-CoA + [Ras]-L-cysteine
[Ras]-S-palmitoyl-L-cysteine + CoA
-
yeast Ras protein is a substrate of Erf2
-
-
r
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [RGS4]-L-cysteine
[RGS4]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [rhodopsin]-L-cysteine
[rhodopsin]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
-
minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
-
-
r
palmitoyl-CoA + [short lipid-modified cysteinyl-containing peptide]-L-cysteine
[short lipid-modified cysteinyl-containing peptide]-S-palmitoyl-L-cysteine + CoA
-
minimum requirements for substrate recognition are a free cysteine thiol adjacent to a hydrophobic lipid anchor, either myristate or farnesyl isoprenoid, overview
-
-
r
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Sna4 protein]-L-cysteine
[Sna4 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
-
-
-
r
palmitoyl-CoA + [SNAP-25]-L-cysteine
[SNAP-25]-S-palmitoyl-L-cysteine + CoA
substrate of DHHC3 and DHHC7
-
-
r
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Snc1]-L-cysteine
[Snc1]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Syn8]-L-cysteine
[Syn8]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Tlg1]-L-cysteine
[Tlg1]-S-palmitoyl-L-cysteine + CoA
-
yeast SNARES Snc1, Syn8, and Tlg1 are substrates of Swf1, palmitoylating at cysteine residues near the cytoplasmic side of their single transmembrane span
-
-
r
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Vac8 protein]-L-cysteine
[Vac8 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modiĀ¢cation
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant Vac8p is palmitoylated when added to vacuoles and is anchored to membranes after modiĀ¢cation
-
-
r
palmitoyl-CoA + [Vac8p]-L-cysteine
[Vac8p]-S-palmitoyl-L-cysteine + CoA
-
recombinant non-myristoylated His6-Vac8p and myristoylated Vac8-GST
-
-
r
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Vac8]-L-cysteine
[Vac8]-S-palmitoyl-L-cysteine + CoA
-
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
-
-
r
palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Yck1 protein]-L-cysteine
[Yck1 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
palmitoyl-CoA + [Ygl108 protein]-L-cysteine
[Ygl108 protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
?
additional information
?
-
-
Kinetics and substrate specificity of PAT, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
in the absence of cellular factors, palmitoyl-CoA is capable of spontaneously S-acylating cysteinyl thiols, overview
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
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
-
-
?
additional information
?
-
-
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
-
-
?
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
-
-
?
additional information
?
-
-
APT1 has acyl-CoA hydrolase activity
-
-
?
additional information
?
-
-
PATis speciĀ¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
-
-
?
additional information
?
-
-
PATis speciĀ¢c for palmitoyl-CoA, since myristoyl- and stearyl-CoA can compete with labeled Pal-CoA only at 10-fold higher amounts
-
-
?
