Characteristics of delta 1-pyrroline-5-carboxylate reductase from Drosophila melanogaster.
1. Biochemical properties of delta 1-pyrroline-5-carboxylate reductase from d. melanogaster have been investigated. 2. The enzyme is stable below 4 degrees C. 3. the pH optimum of the enzyme is 5.7. It is rapidly inactivated below pH 5.4. 4. The Km values for NADPH and delta 1-pyrroline-5-carboxylate are 1.6 x 10-5 and 2.5 x 10-6 M, respectively. 5. the estimated molecular weight of the enzyme is 225,000. 6. the enzyme is weakly inhibited by L-proline (Ki = 0.12 M).
D000818:Animals; D004331:Drosophila melanogaster / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D011762:Pyrroline Carboxylate Reductases / Q000378:metabolism*; D000097502:delta-1-Pyrroline-5-Carboxylate Reductase
D000587:Oxidoreductases Acting on CH-NH Group Donors; D011762:Pyrroline Carboxylate Reductases; D000097502:delta-1-Pyrroline-5-Carboxylate Reductase