Pub. Date : 2021 Nov 30
PMID : 34752700
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 2 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 3 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 4 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 5 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 6 | Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-gamma-semialdehyde dehydrogenase (GSALDH) activities. | Proline | proline dehydrogenase 1 | Homo sapiens |
| 7 | PutA is shown here to catalyze the FAD-dependent PRODH oxidation of both T4C and T2C with catalytic efficiencies significantly higher than with proline. | Proline | proline dehydrogenase 1 | Homo sapiens |