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2.3.1.97: glycylpeptide N-tetradecanoyltransferase

This is an abbreviated version!
For detailed information about glycylpeptide N-tetradecanoyltransferase, go to the full flat file.

Word Map on EC 2.3.1.97

Reaction

tetradecanoyl-CoA
+
an N-terminal-glycyl-[protein]
=
CoA
+
an N-terminal-N-tetradecanoylglycyl-[protein]

Synonyms

CaNMT, cell division control protein 72, dipeptide N-myristoyltransferase 2, glycylpeptide N-tetradecanoyltransferase, glycylpeptide N-tetradecanoyltransferase 1, glycylpeptide N-tetradecanoyltransferase 2, HsNMT1, HsNMT2, LmNMT, More, myristoyl-CoA-protein N-myristoyltransferase, myristoyl-CoA: protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase, myristoyl-CoA:protein N-myristoyltransferase 1, myristoyl-CoA:protein N-myristoyltransferase 2, myristoyl-CoA:protein N-myristoyltransferase type 2, myristoyl-coenzyme A:protein N-myristoyl transferase, myristoyl-coenzyme A:protein N-myristoyltransferase, myristoylating enzymes, myristoyltransferase, myristoyltransferase type 1, myristoyltransferase, protein N-, N-myristoyl transferase, N-myristoyltransferase, N-myristoyltransferase 1, N-myristoyltransferase 2, NMT, NMT 1, NMT 2, NMT-1, NMT-2, NMT1, Nmt1p, NMT2, peptide N-myristoyltransferase, peptide N-myristoyltransferase 1, peptide N-myristoyltransferase 2, protein N-myristoyltransferase, PVX_085815, TbNMT, type I N-myristoyltransferase, type II N-myristoyltransferase

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.97 glycylpeptide N-tetradecanoyltransferase

Application

Application on EC 2.3.1.97 - glycylpeptide N-tetradecanoyltransferase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
drug development
medicine
molecular biology
-
the enzyme can be used for protein N-myristoylation as a tag labeling technique in recombinant expresssion systems. CaNMT is an effective tool for in vitro and in vivo transfer of an azide-modified acid to the N-terminus of a polypeptide derived from a species entirely unrelated to Candida albicans
synthesis
-
recombinant expression of N-myristoylated proteins in Escherichia coli can be achieved by co-expressing N-myristoyltransferase and supplementing the growth medium with myristic acid. Undesired incorporation of the 12-carbon fatty acid lauric acid can also occur, leading to heterogeneous samples. A strategy for obtaining lauryl-free samples of myristoylated proteins in both rich and minimal media