PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1856865-0	1991	Lysozyme revisited: crystallographic evidence for distortion of an N-acetylmuramic acid residue bound in site D. A structure of the trisaccharide 2-acetamido-2-deoxy-D-muramic acid-beta (1----4)-2-acetamido-2-deoxy-D-glucose-beta (1----4)-2-acetamido-2-deoxy-D-muramic acid (NAM-NAG-NAM), bound to subsites B, C and D in the active-site cleft of hen egg-white lysozyme has been determined and refined at 1.5 A resolution.	N-acetylmuramic acid	67-87	lysozyme	Homo sapiens	0-8	
19294463-5	2009	Lysozyme, widely present in body fluids, catalyzes the hydrolysis of beta 1,4 linkage between N-acetyloglucosamine and N-acetylmuramic acid in the bacterial cell wall and cooperates with the complement system in the bactericidal action of serum.	N-acetylmuramic acid	119-139	lysozyme	Homo sapiens	0-8	
35446133-2	2022	Planktonic-phase E. faecalis is resistant to high concentrations of the enzyme lysozyme, which catalyzes the hydrolysis of N-acetylmuramic acid and N-acetylglucosamine linkages in peptidoglycan and is also a cationic antimicrobial peptide (CAMP).	N-acetylmuramic acid	123-143	lysozyme	Homo sapiens	79-87	
35356735-4	2022	Lysozyme exerts antimicrobial activity against microorganisms, especially Gram-positive bacteria, by hydrolyzing 1,4-beta-linkages between N-acetylmuramic acid and N-acetylglucosamine in the cell wall.	N-acetylmuramic acid	139-159	lysozyme	Homo sapiens	0-8	
30818346-2	2019	Among the many applications of lysozyme, the antibacterial activity features caused by the hydrolysis of 1-4 glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine of gram-positive bacteria are beneficial in the food industry, medicine, trade, and pharmacology.	N-acetylmuramic acid	134-154	lysozyme	Homo sapiens	31-39	
30372997-3	2019	It is generally believed that the high efficiency of lysozyme in inhibiting gram-positive bacteria is caused by its ability to cleave the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine.	N-acetylmuramic acid	173-193	lysozyme	Homo sapiens	53-61	
25994146-1	2015	Lysozyme (EC 3.2.1.17) is a hydrolytic enzyme that cleaves the beta-(1,4)-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycan, a major bacterial cell wall polymer.	N-acetylmuramic acid	98-118	lysozyme	Homo sapiens	0-8	
28343137-1	2017	HYPOTHESIS: The interaction of lysozyme with the N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) unit of peptidoglycan (PGN) polymer of the bacterial cell wall is of immense importance to understand the mechanism of lysozyme on PGN.	N-acetylmuramic acid	49-69	lysozyme	Homo sapiens	31-39	
28343137-1	2017	HYPOTHESIS: The interaction of lysozyme with the N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) unit of peptidoglycan (PGN) polymer of the bacterial cell wall is of immense importance to understand the mechanism of lysozyme on PGN.	N-acetylmuramic acid	49-69	lysozyme	Homo sapiens	225-233	
28343137-1	2017	HYPOTHESIS: The interaction of lysozyme with the N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) unit of peptidoglycan (PGN) polymer of the bacterial cell wall is of immense importance to understand the mechanism of lysozyme on PGN.	N-acetylmuramic acid	71-74	lysozyme	Homo sapiens	31-39	
28343137-1	2017	HYPOTHESIS: The interaction of lysozyme with the N-acetylmuramic acid (NAM) and N-acetylglucosamine (NAG) unit of peptidoglycan (PGN) polymer of the bacterial cell wall is of immense importance to understand the mechanism of lysozyme on PGN.	N-acetylmuramic acid	71-74	lysozyme	Homo sapiens	225-233