PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
16038618-3	2005	Using intrinsic tryptophan fluorescence [Castro, Gratson, Evans, Jiracek, Collinsova, Ludwig and Garrow (2004) Biochemistry 43, 5341-5351], it was shown that BHMT exists in three steady-state conformations: enzyme alone, enzyme plus occupancy at the first substrate-binding site (Hcy or Met), or enzyme plus occupancy at both substrate-binding sites (Hcy plus betaine, or Hcy plus DMG).	Tryptophan	16-26	betaine--homocysteine S-methyltransferase	Homo sapiens	158-162	
15122900-6	2004	Mutation of each of the seven tryptophan residues in human BHMT provides evidence that the enzyme undergoes two distinct conformational changes that are reflected in the fluorescence of the enzyme.	Tryptophan	30-40	betaine--homocysteine S-methyltransferase	Homo sapiens	59-63	
15122900-0	2004	Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis.	Tryptophan	99-109	betaine--homocysteine S-methyltransferase	Homo sapiens	38-78	
15122900-3	2004	Using changes in intrinsic tryptophan fluorescence to determine the affinity of human BHMT for substrates, products, or CBHcy, we now demonstrate that the enzyme-substrate complex reaches its transition state through an ordered bi-bi mechanism in which Hcy is the first substrate to bind and Met is the last product released.	Tryptophan	27-37	betaine--homocysteine S-methyltransferase	Homo sapiens	86-90