PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10880957-6	2000	Holoenzyme formation in the presence of FAD increased linearly with the concentration of matrix protein in the assay, and depended on the amount of externally added Me2GlyDH with saturation characteristics.	Flavin-Adenine Dinucleotide	40-43	dimethylglycine dehydrogenase	Rattus norvegicus	165-173	
18423846-4	2008	Results described here definitively demonstrate that: (i) covalent attachment of FAD to Me(2)GlyDH apoenzyme can proceed in vitro autocatalytically, without third reactants; (ii) the removal of mitochondrial presequence by mitochondrial processing peptidase is not required for covalent autoflavinylation.	Flavin-Adenine Dinucleotide	81-84	dimethylglycine dehydrogenase	Rattus norvegicus	88-98	
4055729-1	1985	The flavoenzymes dimethylglycine dehydrogenase (EC 1.5.99.2) and sarcosine dehydrogenase (EC 1.5.99.1) contain covalently bound FAD linked via the 8 alpha-position of the isoalloxazine ring to the imidazole N(3) of a histidine residue (Cook, R. J., Misono, K. S., and Wagner, C. (1984) J. Biol.	Flavin-Adenine Dinucleotide	128-131	dimethylglycine dehydrogenase	Rattus norvegicus	17-46	
9839943-4	1998	The deduced amino acid sequence of SarDH shares an overall similarity of 47% with dimethylglycine dehydrogenase (Me2GlyDH), another flavoenzyme involved in the mitochondrial choline catabolism with a similar FAD-binding domain.	Flavin-Adenine Dinucleotide	208-211	dimethylglycine dehydrogenase	Rattus norvegicus	113-121	
1710985-18	1991	The N-terminus of Me2GlyDH contains a conserved amino acid sequence which forms the dinucleotide-binding site in many enzymes with noncovalently bound FAD.	Flavin-Adenine Dinucleotide	151-154	dimethylglycine dehydrogenase	Rattus norvegicus	18-26