PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32159324-4	2020	Structures of the bifunctional proline catabolic enzyme proline utilization A (PutA) determined from crystals grown in the presence of T2C feature strong electron density for a 5-membered ring species resembling l-T2C covalently bound to the N5 of the FAD in the PRODH domain.	puta	79-83	proline dehydrogenase 1	Homo sapiens	263-268	
34752700-4	2021	PutA is shown here to catalyze the FAD-dependent PRODH oxidation of both T4C and T2C with catalytic efficiencies significantly higher than with proline.	puta	0-4	proline dehydrogenase 1	Homo sapiens	49-54	
28712849-7	2017	PutA is a large (>1000 residues) bifunctional enzyme that combines PRODH and GSALDH activities into one polypeptide chain.	puta	0-4	proline dehydrogenase 1	Homo sapiens	70-75