2.3.1.142: glycoprotein O-fatty-acyltransferase
This is an abbreviated version!
For detailed information about glycoprotein O-fatty-acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.142
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2.3.1.142
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lysophosphatidylcholine
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transacetylase
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acetoxy
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lpcat2
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gnat
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7,8-diacetoxy-4-methylcoumarin
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acetoxycoumarins
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amp-forming
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autoacetylation
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acyl-coa:lysophosphatidylcholine
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sirtuin-like
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lyso-paf
- 2.3.1.142
- lysophosphatidylcholine
- transacetylase
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acetoxy
- lpcat2
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gnat
- 7,8-diacetoxy-4-methylcoumarin
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acetoxycoumarins
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amp-forming
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autoacetylation
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acyl-coa:lysophosphatidylcholine
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sirtuin-like
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lyso-paf
Reaction
Synonyms
acyltransferase, protein, CRTAase, GlnA1, LPCAT1, MTAase, Pat, PATI, protein acetyltransferase, protein fatty acyltransferase, ras palmitoyl acyltransferase, Ras PAT
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2.3.1.142 glycoprotein O-fatty-acyltransferaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.3.1.142 - glycoprotein O-fatty-acyltransferase
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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
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r
glutathione-S-transferase + 7,8-diacetoxy-4-methylcoumarin
?
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?
glutathione-S-transferase + acetyl-CoA
?
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recombinant Schistosoma japonicum glutathione S-transferase
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?
palmitoyl-CoA + adenylate cyclase toxin
CoA + palmitoyladenylate cyclase toxin
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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
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?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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involved in modification of membrane glycoproteins
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?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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involved in modification of membrane glycoproteins
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?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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?
palmitoyl-CoA + mucus glycoprotein
CoA + O-palmitoylglycoprotein
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involved in modification of membrane glycoproteins
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?
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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?
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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?
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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?
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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?
