TY - JOUR
T1 - MyristoylCoA:protein N‐Myristoyltransferase
T2 - Probing Host‐Guest Interactions Using Synthetic Substrates
AU - Gokel, George W.
AU - Lu, Tianbao
AU - Rudnick, David A.
AU - Jackson‐Machelski, Emily
AU - Gordon, Jeffrey I.
PY - 1992
Y1 - 1992
N2 - MyristoylCoA:protein N‐myristoyl transferase (NMT) catalyzes the cotranslational covalent attachment of myristate (C14:0) to the ammo‐terminal glycine residues of a variety of biologically important proteins. An extensive survey of myristic acid analogs has previously allowed us to infer the conformational constraints imposed upon the fatty acid when bound to the enzyme's acylCoA binding site. A series of myristic acid analogs has now been synthesized and studied in an in vitro assay to probe further the conformation of NMT's bound ligand and to assess the importance of the distance between the carboxyl and the proposed bend in the fatty acid.
AB - MyristoylCoA:protein N‐myristoyl transferase (NMT) catalyzes the cotranslational covalent attachment of myristate (C14:0) to the ammo‐terminal glycine residues of a variety of biologically important proteins. An extensive survey of myristic acid analogs has previously allowed us to infer the conformational constraints imposed upon the fatty acid when bound to the enzyme's acylCoA binding site. A series of myristic acid analogs has now been synthesized and studied in an in vitro assay to probe further the conformation of NMT's bound ligand and to assess the importance of the distance between the carboxyl and the proposed bend in the fatty acid.
UR - http://www.scopus.com/inward/record.url?scp=85005701849&partnerID=8YFLogxK
U2 - 10.1002/ijch.199200017
DO - 10.1002/ijch.199200017
M3 - Article
AN - SCOPUS:85005701849
SN - 0021-2148
VL - 32
SP - 127
EP - 133
JO - Israel Journal of Chemistry
JF - Israel Journal of Chemistry
IS - 1
ER -