PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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