CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.630.170
Functional Family Glycylpeptide N-tetradecanoyltransferase

Enzyme Information

2.3.1.97
Glycylpeptide N-tetradecanoyltransferase.
based on mapping to UniProt P30419
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal- N-tetradecanoylglycyl-[protein].
-!- The enzyme catalyzes the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. -!- It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. -!- The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5.

UniProtKB Entries (1)

P30419
NMT1_HUMAN
Homo sapiens
Glycylpeptide N-tetradecanoyltransferase 1

PDB Structure

PDB 5MU6
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus.
Mousnier, A., Bell, A.S., Swieboda, D.P., Morales-Sanfrutos, J., Perez-Dorado, I., Brannigan, J.A., Newman, J., Ritzefeld, M., Hutton, J.A., Guedan, A., Asfor, A.S., Robinson, S.W., Hopkins-Navratilova, I., Wilkinson, A.J., Johnston, S.L., Leatherbarrow, R.J., Tuthill, T.J., Solari, R., Tate, E.W.
Nat Chem