Ontology highlight
ABSTRACT:
SUBMITTER: Soupene E
PROVIDER: S-EPMC4727424 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Soupene Eric E Kao Joseph J Cheng Daniel H DH Wang Derek D Greninger Alexander L AL Knudsen Giselle M GM DeRisi Joseph L JL Kuypers Frans A FA
Journal of lipid research 20151130 2
The covalent attachment of a 14-carbon aliphatic tail on a glycine residue of nascent translated peptide chains is catalyzed in human cells by two N-myristoyltransferase (NMT) enzymes using the rare myristoyl-CoA (C(14)-CoA) molecule as fatty acid donor. Although, NMT enzymes can only transfer a myristate group, they lack specificity for C(14)-CoA and can also bind the far more abundant palmitoyl-CoA (C(16)-CoA) molecule. We determined that the acyl-CoA binding protein, acyl-CoA binding domain ( ...[more]