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Enzyme Nomenclature
Information on EC 2.3.1.142 - glycoprotein O-fatty-acyltransferase
Word Map on EC 2.3.1.142
- 2.3.1.142
- lysophosphatidylcholine
-
transacetylase
-
calreticulin
-
acetoxy
-
7,8-diacetoxy-4-methylcoumarin
-
gnat
-
acetoxycoumarins
- lpcat2
-
acyl-coa:lysophosphatidylcholine
-
autoacetylation
-
amp-forming
-
lyso-paf
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.3.1.142
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RECOMMENDED NAME
GeneOntology No.
glycoprotein O-fatty-acyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
fatty-acyl-CoA:mucus-glycoprotein fatty-acyltransferase
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CAS REGISTRY NUMBER
COMMENTARY
122191-29-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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
physiological function
additional information
physiological function
-
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
physiological function
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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
physiological function
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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
additional information
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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
additional information
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active site of rGlnA1 for TAase activity, overview
additional information
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the P-domain of recombinant calreticulin, unlike its N- and C-domains, is endowed with CRTAase function
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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
RGS16 + palmitoyl-CoA
O-palmitoyl-RGS16 + CoA
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RGS16 is the regulator of G protein signaling 16
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-
r
tubulin Galphai + palmitoyl-CoA
O-palmitoyl-tubulin Galphai + CoA
-
-
-
-
r
glutathione-S-transferase + 7,8-diacetoxy-4-methylcoumarin
?
-
-
-
-
?
glutathione-S-transferase + acetyl-CoA
?
-
recombinant Schistosoma japonicum glutathione S-transferase
-
-
?
palmitoyl-CoA + adenylate cyclase toxin
CoA + palmitoyladenylate cyclase toxin
-
acyltransferase CyaC palmitoylates the conserved lysines 983 and 860 of adenylate cyclase toxin
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?
palmitoyl-CoA + adenylate cyclase toxin
CoA + palmitoyladenylate cyclase toxin
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palmitoylation activates adenylate cyclase toxin
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
-
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
-
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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protein S-palmitoylation is a posttranslational modification in which a palmitoyl group is added to a protein via a thioester linkage on cysteine
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-
r
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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purified recombinant His6:Erf2-Erf4 complex
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-
r
additional information
?
-
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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
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-
-
additional information
?
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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
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-
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additional information
?
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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
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-
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additional information
?
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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
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additional information
?
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acylation of proteins through the addition of palmitate to a cysteine residue is a common posttranslational modification for a variety of proteins
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-
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additional information
?
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the enzyme shows a preference for palmitate and to a lesser degree for other long-chain fatty acids, overview
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
glutathione-S-transferase + 7,8-diacetoxy-4-methylcoumarin
?
-
-
-
-
?
palmitoyl-CoA + adenylate cyclase toxin
CoA + palmitoyladenylate cyclase toxin
-
palmitoylation activates adenylate cyclase toxin
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
involved in modification of membrane glycoproteins
-
?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
-
protein S-palmitoylation is a posttranslational modification in which a palmitoyl group is added to a protein via a thioester linkage on cysteine
-
-
r
additional information
?
-
-
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
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-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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acylation of proteins through the addition of palmitate to a cysteine residue is a common posttranslational modification for a variety of proteins
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
octyl-beta-D-glucoside
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at concentrations below its critical micellar concentration
additional information
-
L-methionine-S-sulfoximine, a potent inhibitor of GlnA1, and a structural analogue of glutamate, fails to inhibit TAase activity of rGlnA1
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1
7,8-diacetoxy-4-methylcoumarin
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pH 6.5, 37°C, recombinant GlnA1
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the addition of different long-chain fatty acids to proteins is cell-type specific
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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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rough microsomes, integral part of rough endoplasmic reticulum, exposed to cytoplasmic side
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rough microsomes, integral part of rough endoplasmic reticulum, exposed to cytoplasmic side
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-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is inactivated by degrading or denaturaring agents, instable during final gel filtration purification step
-
Erf4 and the C-terminal 58 amino acids of Erf2 are required for Erf2 stability
-
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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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
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
co-overexpression of His-tagged Erf2 with fused FLAG-tagged Erf4 in strain RJY1827, expression of FLAG-tagged Erf2 in strain RJY
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expression of wild-type CyaC acyltransferase and various mutants in Escherichia coli
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gene glnA1 or Rv2220, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A140G
-
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
A140V
-
monoacetylation of adenylate cyclase toxin almost exclusively at Lys983
additional information
-
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
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.142)
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