PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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	
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	
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