PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34053981-2	2021	Here we demonstrate the chemoenzymatic syntheses of 4-coumaroyl- and hexanoyl-amino acids, using 4-coumarate: coenzyme A ligase from the model plant Arabidopsis thaliana (At4CL2).	Coumaric Acids	97-108	4-coumarate:CoA ligase 2	Arabidopsis thaliana	171-177	
21393854-1	2011	4-Coumarate:CoA ligase 2 (4CL2) from Arabidopsis thaliana catalyzes the ATP-dependent formation of the 4-coumaroyl-CoA thioester through the formation of 4-coumarate-AMP.	Coumaric Acids	0-11	4-coumarate:CoA ligase 2	Arabidopsis thaliana	26-30	
14769935-3	2004	The encoded enzyme, At4CL4, exhibits the rare property of efficiently activating sinapate, besides the usual 4CL substrates (4-coumarate, caffeate, and ferulate), indicating a distinct metabolic function.	Coumaric Acids	125-136	4-coumarate:CoA ligase 2	Arabidopsis thaliana	22-25	
11576429-0	2001	Identification of 4-coumarate:coenzyme A ligase (4CL) substrate recognition domains.	Coumaric Acids	18-29	4-coumarate:CoA ligase 2	Arabidopsis thaliana	49-52