Pub. Date : 2020 Apr 17
PMID : 32159324
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 2 | Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 3 | Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 4 | Proline dehydrogenase (PRODH) catalyzes the first step of proline catabolism, the FAD-dependent 2-electron oxidation of l-proline to Delta1-pyrroline-5-carboxylate. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 5 | Here we show that the proline analogue thiazolidine-2-carboxylate (T2C) is a mechanism-based inactivator of PRODH. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 6 | 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. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 7 | 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. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 8 | These results may inform the design of new mechanism-based inactivators of PRODH for use as chemical probes to study the roles of proline metabolism in cancer. | Proline | proline dehydrogenase 1 | Homo sapiens |