PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28026940-1	2017	Serum paraoxonase 1 (PON1) is a native lactonase capable of promiscuously hydrolyzing a broad range of substrates, including organophosphates, esters, and carbonates.	Esters	143-149	paraoxonase 1	Homo sapiens	21-25	
14695884-6	2004	In particular, we have evolved PON1 variants with OP-hydrolyzing activities 40-fold higher than wild type and a specificity switch of >2,000-fold, producing PONs specialized for OP rather than ester hydrolysis.	Esters	196-201	paraoxonase 1	Homo sapiens	31-35	
31947900-1	2020	Mammalian paraoxonase-1 hydrolyses a very broad spectrum of esters such as certain drugs and xenobiotics.	Esters	60-66	paraoxonase 1	Homo sapiens	10-23	
22193970-1	2012	Human paraoxonase 1 (huPON1) is a calcium-dependent esterase responsible for hydrolysis of a wide variety of substrates including organophosphates, esters, lactones, and paraoxon.	Esters	148-154	paraoxonase 1	Homo sapiens	6-19	
19945920-4	2010	PON1 displays two distinct catalytic behaviors, one against esters and lactones, the other against organophosphorus compounds; its functional states and catalytic activities against these substrates are differently modulated by the molecular environment; PON1 exists under several active multimeric forms; the binding of HPBP amends the size of the oligomeric states and exerts a stabilizing effect on the activities of PON1; PON1 functional properties are modulated by HPBP, calcium and phosphate.	Esters	60-66	paraoxonase 1	Homo sapiens	0-4	
16595195-1	2006	Human plasma paraoxonase (PON1) is calcium-dependent enzyme that hydrolyses esters, including organophosphates and lactones, and exhibits anti-atherogenic properties.	Esters	76-82	paraoxonase 1	Homo sapiens	26-30	
19082953-1	2008	Mammalian paraoxonases (PON1, PON2, PON3) are a unique family of calcium-dependent hydrolases, with enzymatic activities toward a broad range of substrates (lactones, thiolactones, carbonates, esters, phosphotriesters).	Esters	193-199	paraoxonase 1	Homo sapiens	24-28	
16331452-1	2006	Human serum paraoxonase 1 (hPON1) belongs to a family of enzymes that catalyze the hydrolysis of a broad range of esters and lactones.	Esters	114-120	paraoxonase 1	Homo sapiens	27-32	
15835926-5	2005	To elucidate the substrate preference and other details of PON1 mechanism of catalysis, structure-activity studies were performed with three groups of substrates that are known to be hydrolyzed by PON1: phosphotriesters, esters, and lactones.	Esters	213-219	paraoxonase 1	Homo sapiens	59-63	
15835926-5	2005	To elucidate the substrate preference and other details of PON1 mechanism of catalysis, structure-activity studies were performed with three groups of substrates that are known to be hydrolyzed by PON1: phosphotriesters, esters, and lactones.	Esters	213-219	paraoxonase 1	Homo sapiens	197-201