PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 32108178-3 2020 Acyl-CoAs of a chain length compatible with the binding site of the N-myristoyltransferase enzymes (NMT) are competitive inhibitors, and the mechanism protecting these enzymes from unwanted acyl-CoA species requires the acyl-CoA binding protein ACBD6. Acyl Coenzyme A 0-9 N-myristoyltransferase 1 Homo sapiens 100-103 2271666-12 1990 The 2-substituted acyl-CoA analogues, 2-hydroxymyristoyl-CoA, 2-bromomyristoyl-CoA, and 2-fluoromyristoyl-CoA, were synthesized and shown to be competitive inhibitors of NMT in vitro (Ki"s = 45, 450, and 200 nM, respectively). Acyl Coenzyme A 18-26 N-myristoyltransferase 1 Homo sapiens 170-173 8444867-6 1993 However, like myristoyl-CoA synthetase, there is an inverse relationship between acyl chain polarity and the activities of hNmt"s acyl-CoA substrates. Acyl Coenzyme A 130-138 N-myristoyltransferase 1 Homo sapiens 123-127 8169796-2 1994 Biological evaluation of these compounds in an in vitro NMT enzyme assay revealed that the nonhydrolyzable acyl CoA analogue 1 was the most potent inhibitor [inhibitor dissociation constant (Ki) = 24 nM]. Acyl Coenzyme A 107-115 N-myristoyltransferase 1 Homo sapiens 56-59 2271666-15 1990 Of the three acyl-CoA analogues, only 2-fluoromyristoyl-CoA served as a substrate for NMT. Acyl Coenzyme A 13-21 N-myristoyltransferase 1 Homo sapiens 86-89