Proline Dehydrogenase
Mostrando 13-24 de 114 artigos, teses e dissertações.
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13. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: mutation causing constitutive enzyme expression.
A mutation resulting in inducer-independent expression of the proline-degradative enzymes was isolated in the yeast Saccharomyces cerevisiae. Strains carrying the mutation, put3, are partially constitutive for proline oxidase and delta 1-pyrroline-5-carboxylate dehydrogenase when grown on a medium lacking proline and are hyperinducible for both enzyme activi
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14. A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis.
Proline is one of the most common compatible osmolytes in water-stressed plants. The accumulation of proline in dehydrated plants is caused both by the activation of proline biosynthesis and by the inactivation of proline degradation; a decrease in the level of accumulated proline in rehydrated plants is caused both by the inhibition of proline biosynthesis
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15. Nicotinamide Adenine Dinucleotide-dependent Proline Dehydrogenase in Chlorella
An NAD-linked dehydrogenase from Chlorella pyrenoidosa Chick catalyzing the conversion of l-proline to Δ1-pyrroline-5-carboxylic acid was partially purified. Δ1-Pyrroline-5-carboxylic acid was identified as the product by co-chromatography of it and its o-aminobenzaldehyde derivative with authentic compounds. The enzyme is NAD and l-proline specific and is
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16. Genetics of L-proline utilization in Escherichia coli.
L-Azetidine-2-carboxylate (AC) and 3,4-dehydro-D,L-proline (DHP) are toxic L-proline analogs that can be used to select bacterial mutants defective for L-proline transport. Mutants resistant to AC and DHP are defective for proline transport alone (putP mutants), and mutants resistant to AC but not to DHP are defective both in putP and in the closely linked p
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17. Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline.
The initial step in the degradation pathways of proline and hydroxyproline is catalyzed by proline oxidase and hydroxyproline oxidase, yielding delta 1-pyrroline-5-carboxylate and delta 1-pyrroline-3-hydroxy-5-carboxylate, respectively. The second step is the oxidation of delta 1-pyrroline-5-carboxylate to glutamate and delta 1-pyrroline-3-hydroxy-5-carboxyl
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18. Subcellular compartmentation in control of converging pathways for proline and arginine metabolism in Saccharomyces cerevisiae.
Enzymes of proline biosynthesis and proline degradation which act on the same compound, delta 1-pyrroline-5-carboxylate, are physically separated in yeast cells. The enzyme responsible for the final step in proline biosynthesis, pyrroline-5-carboxylate reductase, converts pyrroline-5-carboxylate to proline and is located in the cytoplasm. The last enzyme in
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19. Expression of the putA gene encoding proline dehydrogenase from Rhodobacter capsulatus is independent of NtrC regulation but requires an Lrp-like activator protein.
Four Rhodobacter capsulatus mutants unable to grow with proline as the sole nitrogen source were isolated by random Tn5 mutagenesis. The Tn5 insertions were mapped within two adjacent chromosomal EcoRI fragments. DNA sequence analysis of this region revealed three open reading frames designated selD, putR, and putA. The putA gene codes for a protein of 1,127
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20. Submitochondrial Location and Electron Transport Characteristics of Enzymes Involved in Proline Oxidation
Isolated corn mitochondria (Zea mays cv. B73 × Mo17) were fractionated and the fragments were separated on a 20-45% (weight/weight) continuous sucrose gradient. Soluble enzymes remained at the top of the gradient overlapping with the outer membranes, while inner membrane vesicles and intact inner membranes were distributed farther down the gradient. Proline
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21. Two proline porters in Escherichia coli K-12.
Escherichia coli mutants defective at putP and putA lack proline transport via proline porter I and proline dehydrogenase activity, respectively. They retain a proline uptake system (proline porter II) that is induced during tryptophan-limited growth and are sensitive to the toxic L-proline analog, 3,4-dehydroproline. 3,4-Dehydroproline-resistant mutants der
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22. Genetic and biochemical requirements for chemotaxis to L-proline in Escherichia coli.
Chemotaxis to L-proline was examined by the capillary assay, using a set of Escherichia coli strains bearing well-defined defects in the enzymes of proline transport and utilization. Aspartate taxis was measured as a constitutive, control activity whose receptor and transducer requirements are known. Proline chemotaxis showed a pattern of induction more anal
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23. Regulation of the major proline permease gene of Salmonella typhimurium.
The structural gene for the major proline permease is located in a tight cluster with genes coding for the proline degradative enzymes, proline oxidase and pyrroline-5-carboxylic acid dehydrogenase. Expression of the permease is regulated in parallel with the two degradative enzymes, and all three functions are subject to catabolite repression. Regulatory mu
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24. Effect of proline on lactate dehydrogenase activity: testing the generality and scope of the compatibility paradigm.
The k(cat) and K(m) kinetic parameters of the labile enzyme rabbit muscle lactic dehydrogenase were determined as a function of the concentration of proline, a solute (osmolyte) accumulated in the cells of many organisms to protect them against environmental stresses. Proline is believed to protect against the stress(es) without altering the functional activ