PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31448845-4	2020	Functional analyses of recombinant-purified CRAT proteins demonstrated that both missense variants, located in the acyl-group binding site of the enzyme, severely impair its catalytic function toward acetyl-CoA, and the p.Val569Met variant also toward propionyl-CoA and octanoyl-CoA.	Acetyl Coenzyme A	200-210	carnitine O-acetyltransferase	Homo sapiens	44-48	
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Acetyl Coenzyme A	125-135	carnitine O-acetyltransferase	Homo sapiens	0-27	
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Acetyl Coenzyme A	125-135	carnitine O-acetyltransferase	Homo sapiens	29-33	
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Acetyl Coenzyme A	70-80	carnitine O-acetyltransferase	Homo sapiens	4-31	
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Acetyl Coenzyme A	70-80	carnitine O-acetyltransferase	Homo sapiens	33-37	
32710884-1	2020	Mammalian carnitine acetyltransferase (CrAT) is a mitochondrial enzyme that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine.	Acetyl Coenzyme A	134-144	carnitine O-acetyltransferase	Homo sapiens	10-37	
32710884-1	2020	Mammalian carnitine acetyltransferase (CrAT) is a mitochondrial enzyme that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine.	Acetyl Coenzyme A	134-144	carnitine O-acetyltransferase	Homo sapiens	39-43	
32710884-6	2020	A great preference for ordered binding is supported by stopped-flow double mixing experiments such that premixed CrAT with acetyl-CoA or CoA demonstrated a biphasic decrease in initial rate that produces about a 100-fold attenuation in catalysis.	Acetyl Coenzyme A	123-133	carnitine O-acetyltransferase	Homo sapiens	113-117	
32710884-7	2020	Double mixing experiments also revealed that the CrAT initial rate is inhibited by 50% in approximately 8 s by either acetyl-CoA or CoA premixing.	Acetyl Coenzyme A	118-128	carnitine O-acetyltransferase	Homo sapiens	49-53	
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetyl Coenzyme A	106-116	carnitine O-acetyltransferase	Homo sapiens	0-27	
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetyl Coenzyme A	106-116	carnitine O-acetyltransferase	Homo sapiens	29-33	
22560225-4	2012	By converting acetyl-CoA to its membrane permeant acetylcarnitine ester, CrAT regulates mitochondrial and intracellular carbon trafficking.	Acetyl Coenzyme A	14-24	carnitine O-acetyltransferase	Homo sapiens	73-77