PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24895213-0	2014	Specific potassium ion interactions facilitate homocysteine binding to betaine-homocysteine S-methyltransferase.	Potassium	9-18	betaine--homocysteine S-methyltransferase	Homo sapiens	71-111	
24895213-3	2014	Herein we report that BHMT is activated by potassium ions with an apparent K(M) for K+ of about 100 microM.	Potassium	43-52	betaine--homocysteine S-methyltransferase	Homo sapiens	22-26	
24895213-8	2014	The potassium binding residues in BHMT partially overlap with the previously identified DGG (Asp26-Gly27-Gly28) fingerprint in the Pfam 02574 group of methyltransferases.	Potassium	4-13	betaine--homocysteine S-methyltransferase	Homo sapiens	34-38	
24895213-10	2014	Together, the data herein indicate that the role of potassium ions in BHMT is structural and that potassium ion facilitates the specific binding of homocysteine to the active site of the enzyme.	Potassium	52-61	betaine--homocysteine S-methyltransferase	Homo sapiens	70-74