PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
29066669-7	2017	We then identified KCl as necessary for BAM2 activity.	Potassium Chloride	19-22	beta-amylase 2	Arabidopsis thaliana	40-44
30154813-2	2018	We recently reported that one of these enzymes, BAM2, is catalytically active in the presence of physiological levels of KCl, exhibits sigmoidal kinetics with a Hill coefficient of over 3, is tetrameric, has a putative secondary binding site (SBS) for starch, and is highly co-expressed with other starch metabolizing enzymes.	Potassium Chloride	121-124	beta-amylase 2	Arabidopsis thaliana	48-52
30154813-2	2018	We recently reported that one of these enzymes, BAM2, is catalytically active in the presence of physiological levels of KCl, exhibits sigmoidal kinetics with a Hill coefficient of over 3, is tetrameric, has a putative secondary binding site (SBS) for starch, and is highly co-expressed with other starch metabolizing enzymes.	Starch	252-258	beta-amylase 2	Arabidopsis thaliana	48-52
30154813-2	2018	We recently reported that one of these enzymes, BAM2, is catalytically active in the presence of physiological levels of KCl, exhibits sigmoidal kinetics with a Hill coefficient of over 3, is tetrameric, has a putative secondary binding site (SBS) for starch, and is highly co-expressed with other starch metabolizing enzymes.	Starch	298-304	beta-amylase 2	Arabidopsis thaliana	48-52
30154813-11	2018	Mutating the serine in BAM2 to a glycine resulted in an enzyme with a VMax similar to that of the wild type enzyme but with a 7.5-fold lower KM for soluble starch.	Serine	13-19	beta-amylase 2	Arabidopsis thaliana	23-27
30154813-11	2018	Mutating the serine in BAM2 to a glycine resulted in an enzyme with a VMax similar to that of the wild type enzyme but with a 7.5-fold lower KM for soluble starch.	Glycine	33-40	beta-amylase 2	Arabidopsis thaliana	23-27
30154813-11	2018	Mutating the serine in BAM2 to a glycine resulted in an enzyme with a VMax similar to that of the wild type enzyme but with a 7.5-fold lower KM for soluble starch.	Starch	156-162	beta-amylase 2	Arabidopsis thaliana	23-27
29066669-10	2017	Conserved residues from a diverse set of BAM2 orthologs were mapped onto a homology model of the protein, revealing a large, conserved surface away from the active site that we hypothesize is a secondary carbohydrate-binding site.	Carbohydrates	204-216	beta-amylase 2	Arabidopsis thaliana	41-45
19664588-5	2009	The low activity of BAM2 may be explained by poor glucan binding but absence of BAM4 activity is not.	Glucans	50-56	beta-amylase 2	Arabidopsis thaliana	20-24