PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9724550-0	1998	Arginine-42 and threonine-45 are required for FAD incorporation and catalytic activity in human monoamine oxidase B.	Flavin-Adenine Dinucleotide	46-49	monoamine oxidase B	Homo sapiens	96-115	
9724550-2	1998	The oxidation of these amine substrates requires the cofactor FAD, which is covalently bound to Cys-397 of human MAO B.	Flavin-Adenine Dinucleotide	62-65	monoamine oxidase B	Homo sapiens	113-118	
9724550-3	1998	Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity.	Flavin-Adenine Dinucleotide	118-121	monoamine oxidase B	Homo sapiens	33-38	
9724550-3	1998	Previously, Glu-34 and Tyr-44 of MAO B have been identified as residues which engage in noncovalent interactions with FAD that are required for subsequent covalent FAD binding and generation of catalytic activity.	Flavin-Adenine Dinucleotide	164-167	monoamine oxidase B	Homo sapiens	33-38	
9724550-8	1998	However, conservative substitutions of Arg-42 with lysine or Thr-45 with serine resulted in MAO B variants that retain both partial activity and partial FAD incorporation.	Flavin-Adenine Dinucleotide	153-156	monoamine oxidase B	Homo sapiens	92-97	
9724550-9	1998	These results indicate that Arg-42 and Thr-45 form critical noncovalent interactions with FAD that are required for the subsequent activation of MAO B by covalent coupling of FAD.	Flavin-Adenine Dinucleotide	90-93	monoamine oxidase B	Homo sapiens	145-150	
9724550-9	1998	These results indicate that Arg-42 and Thr-45 form critical noncovalent interactions with FAD that are required for the subsequent activation of MAO B by covalent coupling of FAD.	Flavin-Adenine Dinucleotide	175-178	monoamine oxidase B	Homo sapiens	145-150