PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16362288-0	2006	Physiological role of D-amino acid-N-acetyltransferase of Saccharomyces cerevisiae: detoxification of D-amino acids.	d-amino acids	102-115	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	22-54
16362288-2	2006	We have determined that D-amino acid-N-acetyltransferase (DNT) of the yeast is involved in the detoxification of D-amino acids on the basis of the following findings.	d-amino acids	113-126	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	24-56
16362288-2	2006	We have determined that D-amino acid-N-acetyltransferase (DNT) of the yeast is involved in the detoxification of D-amino acids on the basis of the following findings.	d-amino acids	113-126	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	58-61
16362288-3	2006	When the DNT gene was disrupted, the resulting mutant was far less tolerant to D-amino acids than the wild type.	d-amino acids	79-92	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	9-12
16362288-4	2006	However, when the gene was overexpressed with a vector plasmid p426Gal1 in the wild type or the mutant S. cerevisiae as a host, the recombinant yeast, which was found to show more than 100 times higher DNT activity than the wild type, was much more tolerant to D-amino acids than the wild type.	d-amino acids	261-274	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	202-205
16362288-6	2006	Thus, D-amino acids are toxic to S. cerevisiae but are detoxified with DNT by N-acetylation preceding removal from yeast cells.	d-amino acids	6-19	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	71-74
31478186-5	2019	Firstly, via disruption of HPA3 encoding d-amino acid-N-acetyltransferase, d-methionine was accumulated in vivo and no N-acetyl-d-methionine production was observed.	D-Methionine	75-87	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	27-31
23775086-4	2013	When expressed in Escherichia coli and assayed in vitro, Hpa2 and Hpa3 (from Met-19) acetylated histones and polyamines.	Polyamines	109-119	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	66-70
15375647-4	2004	Hpa3p acts on a wide range of D-amino acids but shows extremely low activity toward histone.	d-amino acids	30-43	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	0-5
15375647-6	2004	Kinetic analyses suggest that Hpa3p catalyzes the N-acetylation of D-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated.	Nitrogen	50-51	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	30-35
15375647-6	2004	Kinetic analyses suggest that Hpa3p catalyzes the N-acetylation of D-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated.	d-amino acids	67-80	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	30-35
15375647-6	2004	Kinetic analyses suggest that Hpa3p catalyzes the N-acetylation of D-amino acids through an ordered bi-bi mechanism, in which acetyl-CoA is the first substrate to be bound and CoA is the last product to be liberated.	Acetyl Coenzyme A	126-136	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	30-35
23775086-7	2013	Hpa3, but not Hpa2, has been reported to acetylate D-amino acids, and we present results consistent with that.	d-amino acids	51-64	D-amino-acid N-acetyltransferase	Saccharomyces cerevisiae S288C	0-4