Proline Dehydrogenase
Mostrando 1-12 de 114 artigos, teses e dissertações.
-
1. Clonagem dos genes putativos para prolina desidrogenase e D1-pirrolina-5-carboxilato desidrogenase de Leishmania (Leishmania) amazonensis e caracterização funcional de seus produtos. / Cloning of genes for putatives proline dehydrogenase and D1-pyrroline- 5-carboxylate dehydrogenase from Leishmania (Leishmania) amazonensis and functional characterization of their products.
Os tripanosomatídeos utilizam aminoácidos, particularmente a prolina, como fontes de carbono e energia. Essas moléculas estão também envolvidas em outros processos fisiológicos como a metaciclogênesis, osmorregulação, ou resistência a diferentes condições de estresse. Duas enzimas, prolina desidrogenase e D1-pirrolina-5-carb
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 28/09/2011
-
2. Characterization of storage proteins, amino acid profile and enzymes involved in lysine metabolism in genetic modified barley (Hordeum vulgare L.) / Caracterização de proteínas de reserva, perfil de aminoácidos e enzimas envolvidas no metabolismo de lisina em cevada (Hordeum vulgare L.) geneticamente modificada
Cereals represent an important source of protein to human food and animal feed. However, they are characterized by low nutritional quality of proteins due to the unbalanced composition of amino acids, caused by the excess of the amino acids proline and glutamine and deficiency of lysine, threonine and tryptophan. The prolamin storage proteins constitute 50%
Publicado em: 2011
-
3. Caracterização molecular e bioquímica da prolina desidrogenase de Trypanosoma cruzi, um possível alvo terapêutico. / Molecular and Biochemical Characterization of the proline dehydrogenase of T. cruzi, a possible therapeutical target .
Os nossos resultados demonstraram a atividade enzimática prolina desidrogenase (PRODH) do produto do gene anotado como codificante de uma prolina oxidase na base dados do genoma de Trypanosoma cruzi. A atividade da proteína codificada por esse gene foi avaliada inicialmente por complementação de uma linhagem de S. cerevisiae deficiente na expressão func
Publicado em: 2010
-
4. Membrane association of proline dehydrogenase in Escherichia coli is redox dependent.
The PutA protein, product of the Escherichia coli gene putA, has two functions essential for proline utilization and for the regulation of putP and putA expression: as the peripheral membrane flavoprotein, proline dehydrogenase (EC 1.5.99.8), it transfers electrons from proline to the respiratory chain, and, as a repressor, it controls expression of genes pu
-
5. Characterization of the Vibrio vulnificus putAP Operon, Encoding Proline Dehydrogenase and Proline Permease, and Its Differential Expression in Response to Osmotic Stress
The Vibrio vulnificus putAP genes encoding a proline dehydrogenase and a proline permease are transcribed in the same direction. Proline dehydrogenase activity and the level of putA transcript were determined to reach a maximum in exponential phase and were then repressed when growth slowed down. Northern blotting and primer extension analyses revealed that
American Society for Microbiology.
-
6. Isolation, DNA sequence analysis, and mutagenesis of a proline dehydrogenase gene (putA) from Bradyrhizobium japonicum.
We report here the cloning and sequencing of the gene for proline dehydrogenase (putA) of Bradyrhizobium japonicum. An open reading frame coding for 1,016 amino acids was identified. The B. japonicum gene codes for a bifunctional protein with proline dehydrogenase and pyrroline-5-carboxylate (P5C) dehydrogenase activities, as it does in Escherichia coli and
-
7. Proline: an essential intermediate in arginine degradation in Saccharomyces cerevisiae.
Results of studies on proline-nonutilizing (Put-) mutants of the yeast Saccharomyces cerevisiae indicate that proline is an essential intermediate in the degradation of arginine. Put- mutants excreted proline when grown on arginine or ornithine as the sole nitrogen source. Yeast cells contained a single enzyme, delta 1-pyrroline-5-carboxylate (P5C) dehydroge
-
8. Genetics and physiology of proline utilization in Saccharomyces cerevisiae: enzyme induction by proline.
Proline is converted to glutamate in the yeast Saccharomyces cerevisiae by the sequential action of two enzymes, proline oxidase and delta 1-pyrroline-5-carboxylate (P5C) dehydrogenase. The levels of these enzymes appear to be controlled by the amount of proline in the cell. The capacity to transport proline is greatest when the cell is grown on poor nitroge
-
9. Regulation of Proline Degradation in Salmonella typhimurium
The pathway for proline degradation in Salmonella typhimurium appears to be identical to that found in Escherichia coli and Bacillus subtilis. Δ1-Pyrroline-5-carboxylic acid (P5C) is an intermediate in the pathway; its formation consumes molecular oxygen. Assays were devised for proline oxidase and the nicotinamide adenine dinucleotide phosphate-specific P5
-
10. Identity of proline dehydrogenase and delta1-pyrroline-5-carboxylic acid reductase in Clostridium sporogenes.
Proline dehydrogenase and delta1-pyrroline-5-carboxylic acid (PCA) reductase activities were copurified 60- and 130-fold, respectively, from extracts of Clostridium sporogenes. The primary change in the ratio of activites was the result of a loss of proline dehydrogenase activity during dialysis. Both activities were eluted in single peaks from diethylaminoe
-
11. Effect of the Proline Analogue Baikiain on Proline Metabolism in Salmonella typhimurium
A proline analogue, 4,5-dehydro-l-pipecolic acid (baikiain) induces the formation in Salmonella typhimurium of the two enzymes catalyzing the degradation of proline, proline oxidase and Δ1-pyrroline-5-carboxylic acid (P5C) dehydrogenase. The level of induction by 20 mm baikiain is about 10% of the maximum level induced by proline. Since the analogue is a su
-
12. Regulation of Arginine and Proline Catabolism in Bacillus licheniformis
The enzymes in the arginine breakdown pathway (arginase, ornithine-δ-transaminase, and Δ′-pyrroline-5-carboxylate dehydrogenase) were found to be present in Bacillus licheniformis cells during exponential growth on glutamate. These enzymes could be coincidentally induced by arginine or ornithine to a very high level and their synthesis could be repressed