PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
34904522-0	2022	Optimal pH 8.5 to 9 for the Hydrolysis of Vixotrigine and Other Basic Substrates of Carboxylesterase-1 in Human Liver Microsomes.	vixotrigine	42-53	carboxylesterase 1	Homo sapiens	84-102	
34904522-2	2022	One of the major in vivo metabolic pathways of vixotrigine in humans is the hydrolysis of the carboxamide to form the carboxylic acid metabolite M14.The in vitro formation of M14 in human hepatocytes was inhibited by the carboxylesterase (CES) inhibitor Bis(4-nitrophenyl) phosphate in a concentration-dependent manner.	vixotrigine	47-58	carboxylesterase 1	Homo sapiens	221-237	
34904522-4	2022	Further investigation has revealed that optimal pH for the hydrolysis of vixotrigine and two other basic substrates of CES1, methylphenidate and oseltamivir, in human liver microsomes was pH 8.5 to 9 which is higher than their respective pKa(base), suggesting that neutral form of basic substrates is probably preferred for CES1 catalysis in liver microsomes.	vixotrigine	73-84	carboxylesterase 1	Homo sapiens	119-123	
34904522-4	2022	Further investigation has revealed that optimal pH for the hydrolysis of vixotrigine and two other basic substrates of CES1, methylphenidate and oseltamivir, in human liver microsomes was pH 8.5 to 9 which is higher than their respective pKa(base), suggesting that neutral form of basic substrates is probably preferred for CES1 catalysis in liver microsomes.	vixotrigine	73-84	carboxylesterase 1	Homo sapiens	324-328