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MyristoylCoA:protein N ‐Myristoyltransferase: Probing Host‐Guest Interactions Using Synthetic Substrates
Author(s) -
Gokel George W.,
Lu Tianbao,
Rudnick David A.,
JacksonMachelski Emily,
Gordon Jeffrey I.
Publication year - 1992
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.199200017
Subject(s) - myristic acid , chemistry , myristoylation , stereochemistry , covalent bond , enzyme , fatty acid , transferase , biochemistry , glycine , amino acid , organic chemistry , palmitic acid , phosphorylation
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.