PMID: 45549Jan 1, 1979

Characteristics of delta 1-pyrroline-5-carboxylate reductase from Drosophila melanogaster

Comparative Biochemistry and Physiology. B, Comparative Biochemistry
J L FarmerC S Smith


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).


Feb 1, 1975·Proceedings of the National Academy of Sciences of the United States of America·S T ThompsonE Stellwagen
Feb 1, 1959·Proceedings of the National Academy of Sciences of the United States of America·T Yura


Feb 13, 2001·Journal of Insect Physiology·S R. MisenerV K. Walker

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PYCR1 protein, human
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Drosophila melanogaster
Enzyme Stability
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Pyrroline Carboxylate Reductases

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