Purification to Homogeneity of Pyrroline-5-Carboxylate Reductase of Barley

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Purification to homogeneity of pyrroline-5-carboxylate reductase of barley.

An enzyme has been purified to homogeneity from barley seedlings which has ;proline dehydrogenase' and the pyrroline-5-carboxylic acid reductase activities. The purification achieved is 39,000-fold as calculated from the proline dehydrogenase activity. The subunit molecular weight of the protein is 30 kilodaltons. The native enzyme has molecular weights up to 480 kilodaltons, depending on the b...

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Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase.

Pyrroline-5-carboxylate reductase (P5CR) catalyzes the reduction of Delta1-pyrroline-5-carboxylate (P5C) to proline with concomitant oxidation of NAD(P)H to NAD(P)(+). The enzymatic cycle between P5C and proline is very important in many physiological and pathological processes. Human P5CR was over-expressed in Escherichia coli and purified to homogeneity by chromatography. Enzymatic assays of ...

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Crystal structure of human pyrroline-5-carboxylate reductase.

Pyrroline-5-carboxylate reductase (P5CR) is a universal housekeeping enzyme that catalyzes the reduction of Delta(1)-pyrroline-5-carboxylate (P5C) to proline using NAD(P)H as the cofactor. The enzymatic cycle between P5C and proline is very important for the regulation of amino acid metabolism, intracellular redox potential, and apoptosis. Here, we present the 2.8 Angstroms resolution structure...

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Pyrroline-5-carboxylate reductase of Neurospora crassa; partial purification and some properties.

Previous studies (1, 2) with mutant and wild type strains of Neurospora crassa have pointed to glutamic y-semialdehyde and its spontaneously cyclized form, Al-pyrroline-5-carboxylate, as intermediates in the biosynthesis of proline. These studies, based largely on experiments in vivo, have recently been substantiated through work in vitro with extracted enzymes (3, 4). ‘The terminal step in pro...

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Pyrroline-5-Carboxylate Reductase in Chlorella autotrophica and Chlorella saccharophila in Relation to Osmoregulation.

Pyrroline-5-carboxylate (P5C) reductase (EC 1.5.1.2), which catalyzes the reduction of P5C to proline, was partially purified from two Chlorella species; Chlorella autotrophica, a euryhaline marine alga that responds to increases in salinity by accumulating proline and ions, and Chlorella saccharophila, which does not accumulate proline for osmoregulation. From the elution profile of this enzym...

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ژورنال

عنوان ژورنال: Plant Physiology

سال: 1986

ISSN: 0032-0889,1532-2548

DOI: 10.1104/pp.80.1.142