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Literature summary extracted from

  • Dunphy, J. T.; Greentree, W. K.; Manahan, C. L.; Linder, M. E.
    G-protein palmitoyltransferase activity is enriched in plasma membranes (1996), J. Biol. Chem., 271, 7154-7159.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.225 membrane
-
 Bos taurus 16020
-
2.3.1.225 additional information low or undetectable levels in Golgi, endoplasmic reticulum, and mitochondria of rat liver, subcellular localization study, overview Rattus norvegicus
-
-
2.3.1.225 additional information no activity in cytosol, subcellular localization study, overview Bos taurus
-
-
2.3.1.225 plasma membrane high enzyme level Rattus norvegicus 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine Bos taurus
-
 [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Rattus norvegicus
-
 [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine Bos taurus
-
 [protein]-S-palmitoyl-L-cysteine + CoA
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.225 Bos taurus
-
-
-
2.3.1.225 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.225 native enzyme from brain membranes partially by gel filtration and anion exchange chromatography Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.225 brain
-
 Bos taurus
-
2.3.1.225 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.225 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 Rattus norvegicus ?
-
 ?
2.3.1.225 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 Bos taurus ?
-
 ?
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine
-
 Bos taurus [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine G protein alpha subunit, wild-type Gia1 and Gia1G203A mutant form heterotrimers with G protein betagammaC68S, myristoylated or not myristoylated Rattus norvegicus [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [Gialpha1]-L-cysteine 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 Bos taurus [Gialpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [GOalpha1]-L-cysteine
-
 Bos taurus [GOalpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [GSalpha1]-L-cysteine Gsa is not a myristoylated protein, but is palmitoylated at Cys3 Bos taurus [GSalpha1]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Rattus norvegicus [protein]-S-palmitoyl-L-cysteine + CoA
-
 r
2.3.1.225 palmitoyl-CoA + [protein]-L-cysteine
-
 Bos taurus [protein]-S-palmitoyl-L-cysteine + CoA
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.3.1.225 Pat
-
 Rattus norvegicus
2.3.1.225 Pat
-
 Bos taurus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.225 30
-
 assay at Rattus norvegicus
2.3.1.225 30
-
 assay at Bos taurus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.225 8
-
 assay at Rattus norvegicus
2.3.1.225 8
-
 assay at Bos taurus

General Information

EC Number General Information Comment Organism
2.3.1.225 additional information role of G-protein betagamma subunits in substrate affinity for PAT may be to provide a mechanism for substrate presentation to PAT. Bos taurus
2.3.1.225 physiological function the enzyme has a role for regulated cycles of acylation and deacylation accompanying activation of G-protein signal transduction pathways Rattus norvegicus
2.3.1.225 physiological function the enzyme has a role for regulated cycles of acylation and deacylation accompanying activation of G-protein signal transduction pathways Bos taurus