PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
29787766-6	2018	The H112N mutant was found to be dimeric, but devoid of catalytic activity, due to the loss of the catalytically essential histidine; nevertheless, it exhibited high affinity to AMP and a HINT1 inhibitor.	Adenosine Monophosphate	178-181	histidine triad nucleotide binding protein 1	Homo sapiens	188-193	
25199874-7	2014	CONCLUSIONS: The enzymatic conversion of AMPS to AMP occurred with the participation of cellular Hint1, the protein, which is present in all organisms.	Adenosine Monophosphate	41-44	histidine triad nucleotide binding protein 1	Homo sapiens	97-102	
26750483-5	2016	Here, the structure of HINT from Helicobacter pylori (HpHINT) in complex with AMP is reported at a resolution of 3 A.	Adenosine Monophosphate	78-81	histidine triad nucleotide binding protein 1	Homo sapiens	23-27	
20499681-2	2010	Hint1 catalyses the process of hydrolysis of the P-N bond in AMP-lysine, AMP-alanine, AMP-NH2.	Adenosine Monophosphate	61-64	histidine triad nucleotide binding protein 1	Homo sapiens	0-5	
22329685-6	2012	Because Ap(4)A can result from condensation of other aa-AMP"s with ATP, the specificity of the Hint1 aa-AMP-hydrolysis activity is of interest.	Adenosine Monophosphate	56-59	histidine triad nucleotide binding protein 1	Homo sapiens	95-100	
23614568-7	2013	We have conducted the first detailed kinetic mechanistic studies of hHint1 and have found that the reaction mechanism is consistent with a double-displacement mechanism, in which the active site nucleophile His112 is first adenylylated by the substrate, followed by hydrolysis of the AMP-enzyme intermediate.	Adenosine Monophosphate	284-287	histidine triad nucleotide binding protein 1	Homo sapiens	68-74	
22869114-3	2012	Here, the structure of the human HINT1-adenosine 5"-monophosphate (AMP) complex at 1.38 A resolution obtained from a new monoclinic crystal form is reported.	Adenosine Monophosphate	67-70	histidine triad nucleotide binding protein 1	Homo sapiens	33-38	
20940308-4	2010	An additional, but usually ignored, activity of Hint-1 is its ability to catalyze the conversion of adenosine 5"-O-monophosphorothioate (AMPS) to 5"-O-monophosphate (AMP).	Adenosine Monophosphate	137-140	histidine triad nucleotide binding protein 1	Homo sapiens	48-54	
17337452-11	2007	Taken together, these results demonstrate that for hHint1; 1) the efficiency (k(cat)/K(m)) of acylated AMP hydrolysis, but not maximal catalytic turnover (k(cat)), is dependent on homodimerization and 2) the hydrolysis of lysyl-AMP generated by LysRS is not dependent on homodimerization if the monomer structure is similar to the wild-type structure.	Adenosine Monophosphate	103-106	histidine triad nucleotide binding protein 1	Homo sapiens	51-57	
15790557-3	2005	Disease-associated mutations in Aprataxin target a histidine triad domain that is similar to Hint, a universally conserved AMP-lysine hydrolase, or truncate the protein NH2-terminal to a zinc finger.	Adenosine Monophosphate	123-126	histidine triad nucleotide binding protein 1	Homo sapiens	93-97