EC Number   |
Natural Substrates |
|---|
   2.3.1.142 | glutathione-S-transferase + 7,8-diacetoxy-4-methylcoumarin |
- |
| 2.3.1.142 | more |
acylation of proteins through the addition of palmitate to a cysteine residue is a common posttranslational modification for a variety of proteins |
| 2.3.1.142 | more |
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 |
| 2.3.1.142 | more |
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 |
| 2.3.1.142 | more |
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 |
| 2.3.1.142 | palmitoyl-CoA + adenylate cyclase toxin |
palmitoylation activates adenylate cyclase toxin |
| 2.3.1.142 | palmitoyl-CoA + mucus glycoprotein |
involved in modification of membrane glycoproteins |
| 2.3.1.142 | palmitoyl-CoA + mucus glycoprotein |
protein S-palmitoylation is a posttranslational modification in which a palmitoyl group is added to a protein via a thioester linkage on cysteine |
