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Information on EC 2.3.1.225 - protein S-acyltransferase and Organism(s) Bos taurus
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2.3.1.225 protein S-acyltransferaseIUBMB 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.
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Word Map
- 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
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
hip14, dhhc3, palmitoyl acyltransferase, dhhc5, zdhhc5, dhhc2, akr1p, zdhhc3, protein acyltransferase, dhhc protein, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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.
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
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 Galphai]-L-cysteine
[G-protein alpha subunit Galphai]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
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 + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
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
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 + [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 + [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
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
palmitoyl-CoA + [G protein alpha subunit]-L-cysteine
[G protein alpha subunit]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [G-protein alpha subunit Galphai]-L-cysteine
[G-protein alpha subunit Galphai]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [Gialpha1]-L-cysteine
[Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
r
palmitoyl-CoA + [protein]-L-cysteine
[protein]-S-palmitoyl-L-cysteine + CoA
-
-
-
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-CoA binding protein
-
i.e. ACBP strongly suppress non-enzymatic thioacylation of cysteinyl containing peptides by long-chain acyl-CoAs, usage of purified rat and recombinant bovine liver ACBP. ACBP only modestly inhibits enzymatic thioacylation of a myristoylated peptide or G-protein K-subunits under conditions where non-enzymatic thioacylation is reduced to background
-
additional information
-
depletion of cellular cholesterol with the drug methyl-beta-cyclodextrin results in inhibition of palmitoyltransferase activity and a redistribution of the remaining activity to membranes of higher density, the process is reversible by cholesterol addition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acyl-CoA binding protein
-
i.e. ACBP strongly suppress non-enzymatic thioacylation of cysteinyl containing peptides by long-chain acyl-CoAs, usage of purified rat and recombinant bovine liver ACBP. ACBP only modestly inhibits enzymatic thioacylation of a myristoylated peptide or G-protein K-subunits under conditions where non-enzymatic thioacylation is reduced to background
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics and substrate specificity of PAT, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
no activity in cytosol, subcellular localization study, overview
-
-
PAT activity is highly enriched in low density membranes dependent upon cholesterol
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
depletion of cellular cholesterol with the drug methyl-beta-cyclodextrin results in inhibition of palmitoyltransferase activity and a redistribution of the remaining activity to membranes of higher density, the process is reversible by cholesterol addition
physiological function
additional information
-
role of G-protein betagamma subunits in substrate affinity for PAT may be to provide a mechanism for substrate presentation to PAT.
physiological function
-
palmitoyltransferase facilitates the enrichment of fatty acylated signaling molecules in plasma membrane subdomains. Fatty acylation, involving the enzyme, is one mechanism for targeting proteins to lipid rafts, low density, sphingomyelin- and cholesterol-enriched membranes. When reconstituted into cell membranes, the population of purified recombinant Gi that is palmitoylated is highly enriched in the low density membrane fractions, whereas the bulk unmodified Gi-protein is largely excluded, the effect requires palmitoyltransferase activity and is abolished if the palmitoylated cysteine was mutated.
physiological function
-
reversible modification by palmitate is a feature of many signaling proteins that are associated with the cytoplasmic leaflet of the plasma membrane
physiological function
-
the enzyme has a role for regulated cycles of acylation and deacylation accompanying activation of G-protein signal transduction pathways
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ZDHC9_BOVIN
363
4
40826
Swiss-Prot
Mitochondrion (Reliability: 5)
ZDHC4_BOVIN
343
5
39710
Swiss-Prot
Secretory Pathway (Reliability: 1)
ZDHC5_BOVIN
714
4
76976
Swiss-Prot
Secretory Pathway (Reliability: 2)
ZDHC6_BOVIN
413
4
47531
Swiss-Prot
Secretory Pathway (Reliability: 5)
GLNA_BOVIN
373
0
42031
Swiss-Prot
other Location (Reliability: 3)
ZDH16_BOVIN
377
4
43614
Swiss-Prot
Mitochondrion (Reliability: 4)
ZDH20_BOVIN
365
4
41907
Swiss-Prot
Secretory Pathway (Reliability: 1)
ZDH21_BOVIN
265
4
31463
Swiss-Prot
Secretory Pathway (Reliability: 1)
Q2KIP1_BOVIN
365
4
41040
TrEMBL
Secretory Pathway (Reliability: 3)
A0A452DIT2_BOVIN
398
4
45863
TrEMBL
Secretory Pathway (Reliability: 1)
E1BPA5_BOVIN
284
5
30305
TrEMBL
Secretory Pathway (Reliability: 1)
A6QNQ5_BOVIN
547
6
62899
TrEMBL
other Location (Reliability: 2)
E1BJK1_BOVIN
632
6
72640
TrEMBL
other Location (Reliability: 1)
E1BK60_BOVIN
488
4
53230
TrEMBL
other Location (Reliability: 4)
E1BDY0_BOVIN
324
4
37994
TrEMBL
Secretory Pathway (Reliability: 1)
F1N6U3_BOVIN
308
4
34983
TrEMBL
other Location (Reliability: 2)
A0A3Q1M403_BOVIN
372
0
41949
TrEMBL
other Location (Reliability: 3)
E1BC01_BOVIN
429
6
48568
TrEMBL
other Location (Reliability: 2)
E1B6X9_BOVIN
268
4
30804
TrEMBL
Secretory Pathway (Reliability: 1)
F1MVC6_BOVIN
288
4
32874
TrEMBL
other Location (Reliability: 4)
Q08DX8_BOVIN
299
4
34186
TrEMBL
other Location (Reliability: 4)
G3MXF3_BOVIN
366
4
41867
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3Q1LVW6_BOVIN
622
7
71066
TrEMBL
other Location (Reliability: 3)
E1BKA0_BOVIN
343
5
39680
TrEMBL
Secretory Pathway (Reliability: 1)
E1B987_BOVIN
263
4
29331
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1LTI4_BOVIN
604
4
69255
TrEMBL
other Location (Reliability: 1)
A0A3Q1N3K0_BOVIN
376
4
43386
TrEMBL
Mitochondrion (Reliability: 4)
E1B8S9_BOVIN
753
4
80199
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3Q1NB78_BOVIN
381
4
42057
TrEMBL
other Location (Reliability: 4)
E1BE85_BOVIN
454
4
49890
TrEMBL
other Location (Reliability: 3)
F1MPF2_BOVIN
344
3
39300
TrEMBL
other Location (Reliability: 4)
G5E6N4_BOVIN
383
4
41750
TrEMBL
other Location (Reliability: 2)
A0A3Q1NJ45_BOVIN
375
4
43109
TrEMBL
Secretory Pathway (Reliability: 1)
G3X756_BOVIN
280
2
29432
TrEMBL
other Location (Reliability: 4)
F1MCX6_BOVIN
631
6
72379
TrEMBL
other Location (Reliability: 2)
A0A3Q1M794_BOVIN
368
4
42086
TrEMBL
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from brain membranes partially by gel filtration and anion exchange chromatography
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Veit, M.; Sachs, K.; Heckelmann, M.; Maretzki, D.; Hofmann, K. P.; Schmidt, M. F. G.
Palmitoylation of rhodopsin with S-protein acyltransferase: enzyme catalyzed reaction versus autocatalytic acylation
Biochim. Biophys. Acta
1394
90-98
1998
Bos taurus
Dunphy, J.T.; Schroeder, H.; Leventis, R.; Greentree, W.K; Knudsen, J.K.; Silvius, J.R.; Linder, M.E.
Differential effects of acyl-CoA binding protein on enzymatic and non-enzymatic thioacylation of protein and peptide substrates
Biochim. Biophys. Acta
1485
185-198
2000
Chlorocebus aethiops, Bos taurus
Dunphy, J. T.; Greentree, W. K.; Manahan, C. L.; Linder, M. E.
G-protein palmitoyltransferase activity is enriched in plasma membranes
J. Biol. Chem.
271
7154-7159
1996
Bos taurus, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 2.3.1.225)
Transporter Classification Database (TCDB): 8.A.114.1.5, 8.A.114.1.3, 8.A.114.1.7, 8.A.114.1.1, 8.A.114.1.2, 8.A.114.1.6, 8.A.114.1.4
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