in the absence of Erf4, the rate of hydrolysis of the active site palmitoyl thioester intermediate is increased, resulting in reduced palmitoyl transfer to a Ras2 substrate
histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decrease cellular mRNA synthesis
palmitoylation is a reversible modification involved in protein membrane targeting, receptor trafficking and signaling, vesicular biogenesis and trafficking, protein aggregation, and protein degradation. An example of the dynamic nature of this modification is the palmitoylation-depalmitoylation cycle that regulates the subcellular trafficking of Ras family GTPases. The Ras protein acyltransferase consists of a complex of Erf2-Erf4 in yeast cells. Both subunits Erf2 and Erf4 are required for PAT activity, one role of Erf4 is to regulate Erf2 stability through an ubiquitin-mediated pathway. Erf4 is required for the stable formation of the palmitoyl-Erf2 intermediate, the first step of palmitoyl transfer to protein substrates
GlnA1 is a virulence determinant factor. The extracellular secretion of GlnA1 in large amounts is thought to play an important role in the biosynthesis of poly L-glutamate/glutamine cell wall
Erf4 and the C-terminal 58 amino acids of Erf2 are required for Erf2 stability. Role of the quality control system in degrading Erf2 molecules that are not in complex with Erf4. The C-terminal 58-amino acid residues of Erf2 are necessary and sufficient for ubiquitin-dependent, ERAD-mediated clearance of DHHC PATs
protein acyltransferase function of purified calreticulin. The rhCRTAase/P-domain also undergoes autoacylation by acyloxycoumarins. The isolated autoacylated rhCRTAase/P-domain in non-denatured form alone exhibits the ability to transfer acyl group to rGST indicating the stable intermediate nature of the acylated enzyme
P-domain catalyzed acetylation of rGST by 7,8-diacetoxy-4-methylcoumarin or acetyl-CoA results in the modification of several lysine residues, LC-MS/MS analysis. Residues Lys173 and Lys174 are present in the P-domain, and are responsible for binding of acyloxycoumarins and acetyl-CoA, they are probably part of the active site
histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decreases cellular mRNA synthesis
besides glutamine synthetase activity, recombinant glutamine synthetase, GlnA1, of Mycobacterium tuberculosis shows additional MTAase function. MTAase exhibits differential specificities to several acyloxycoumarins, and is also capable of transferring propionyl and butyryl groups from propoxy and butoxy derivatives of 4-methylcoumarin, detailed overview. MTAase fails to accept as substrates the compounds bearing acetoxy group on the lactone ring at C-3/C-4 position of coumarin
protein acyltransferase function of purified calreticulin. The rhCRTAase/P-domain also undergoes autoacylation by acyloxycoumarins. The isolated autoacylated rhCRTAase/P-domain in non-denatured form alone exhibits the ability to transfer acyl group to rGST indicating the stable intermediate nature of the acylated enzyme
histone H4 protein is subject to palmitoylation catalyzed by Lpcat1 in a calcium-regulated manner. Cytosolic Lpcat1 shifts into the nucleus in lung epithelia in response to exogenous Ca2+. Nuclear Lpcat1 colocalizes with and binds to histone H4, where it catalyzes histone H4 palmitoylation. Residue Ser47 within histone H4 serves as a putative acceptor site, indicative of Lpcat1-mediated O-palmitoylation. Lpcat1 knock-down or expression of a histone H4 Ser47A mutant protein in cells decreases cellular mRNA synthesis
besides glutamine synthetase activity, recombinant glutamine synthetase, GlnA1, of Mycobacterium tuberculosis shows additional MTAase function. MTAase exhibits differential specificities to several acyloxycoumarins, and is also capable of transferring propionyl and butyryl groups from propoxy and butoxy derivatives of 4-methylcoumarin, detailed overview. MTAase fails to accept as substrates the compounds bearing acetoxy group on the lactone ring at C-3/C-4 position of coumarin
the Erf2-Erf4 complex localizes to the endoplasmic reticulum where it palmitoylates Ras. Role of the quality control system in degrading Erf2 molecules that are not in complex with Erf4
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, partially purified enzyme, 0.15% v/v Triton X-100, 150 mM KCl, 20 mM Tris-HCl, pH 7.4, 1 mM EGTA, 0.01 mg/ml leupeptin, at least 3 months without loss of activity
partial, 95fold from liver by preparation of plasma membrane fraction, solubilization with 0.15% Triton X-100, and sequential chromatography including affinity chromatography on a cerulin-based palmitoylation inhibitor ligand
recombinant His-tagged Erf2 with fused FLAG-tagged Erf4 from strain RJY1827, solubilization by 0.8% dodecylmaltoside and urea, and ultracentrifugation, purification by nickel affinity chromatography and desalting gel filtration, recombinant FLAG-tagged Erf2 by the same method
changed selectivity of acyltransferase for the 2 acetylation sites of adenylate cyclase toxin, a mixture of bi and monoacetylated toxins modified either at both Lys860 and Lys983 or only at Lys860 is generated
construction of a fusion protein that places the 58 amino acids of Erf2 onto the C-terminus of Pfa4, another DHHC enzyme that resides in the endoplasmic reticulum membrane, the modification highly reduces the half-life of the engineered protein
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
Patt1, a novel protein acetyltransferase that is highly expressed in liver and downregulated in hepatocellular carcinoma, enhances apoptosis of hepatoma cells.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
Lysophosphatidylcholine acyltransferase 1 (LPCAT1) upregulation in breast carcinoma contributes to tumor progression and predicts early tumor recurrence.
LPS impairs phospholipid synthesis by triggering beta-transducin repeat-containing protein (beta-TrCP)-mediated polyubiquitination and degradation of the surfactant enzyme acyl-CoA:lysophosphatidylcholine acyltransferase I (LPCAT1).
Basar, T.; Havlicek, V.; Bezouskova, S.; Hackett, M.; Sebo, P.
Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC
The erf4 subunit of the yeast ras palmitoyl acyltransferase is required for stability of the acyl-erf2 intermediate and palmitoyl transfer to a ras2 substrate
Protein acyltransferase function of purified calreticulin: the exclusive role of P-domain in mediating protein acylation utilizing acyloxycoumarins and acetyl CoA as the acyl group donors