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119 results on '"Ruggieri, Silverio"'

1. Food Quality and Functionality

Author

Pacetti, Deborah, Mezzetti, Bruno, Balducci, Francesca, Balzano, Michele, Carloni, Patricia, Castiglioni, Sara, Cianci, Michele, Falcone, Pasquale Massimiliano, Frega, Natale Giuseppe, Giardinieri, Alessandra, Mazzoni, Luca, Minazzato, Gabriele, Raffaelli, Nadia, Ruggieri, Silverio, Zamporlini, Federica, Longhi, Sauro, editor, Monteriù, Andrea, editor, Freddi, Alessandro, editor, Aquilanti, Lucia, editor, Ceravolo, Maria Gabriella, editor, Carnevali, Oliana, editor, Giordano, Mario, editor, and Moroncini, Gianluca, editor

Published
2020
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9. Enzymology of Nad+Synthesis

Author

Magni, Giulio, primary, Amici, Adolfo, additional, Emanuelli, Monica, additional, Raffaelli, Nadia, additional, and Ruggieri, Silverio, additional

Published
2006
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10. The Escherichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltrasferase activity

Author

Raffaelli, Nadia, Lorenzi, Teresa, Mariani, P. Luigi, Emanuelli, Monica, Amici, Adolfo, Ruggieri, Silverio, and Magni, Giulio

Subjects
Bacteriology -- Research, Escherichia coli -- Research, NAD (Coenzyme) -- Research, Catalysts -- Research, Cloning -- Research, Biological sciences
Abstract

Research has been conducted on the identification of NadR protein catalytic activity. Cloning and expression of Escherichia coli nadR gene to investigate its possible nicotinamide mononucleotide adenylyltransferase activity is discussed.

Published
1999

13. Characterization of nicotinamide mononucleotide adenylyltransferase from thermophilic archaea

Author

Raffaelli, Nadia, Pisani, Francesca M., Lorenzi, Teresa, Emanuelli, Monica, Amici, Adolfo, Ruggieri, Silverio, and Magni, Giulio

Subjects
Enzymes -- Research, Bacteria, Thermophilic -- Research, Biological sciences
Abstract

Research was conducted to describe the characterization of the nicotinamide mononucleotide adenylyltransferase enzyme from thermophilic archaea. Sulfolobus solfataricus cells were grown on glucose as the carbon source and were collected at the stationary phase. Moreover, expressed proteins were purified to homogeneity by a single-step chromatographic method. Results showed that the n-terminal sequence of the S. solfataricus protein helped in identifying the archaeal enzyme gene.

Published
1997

31. Identification of Nicotinamide Mononucleotide Deamidase of the Bacterial Pyridine Nucleotide Cycle Reveals a Novel Broadly Conserved Amidohydrolase Family

Author

Galeazzi, Luca, primary, Bocci, Paola, additional, Amici, Adolfo, additional, Brunetti, Lucia, additional, Ruggieri, Silverio, additional, Romine, Margaret, additional, Reed, Samantha, additional, Osterman, Andrei L., additional, Rodionov, Dmitry A., additional, Sorci, Leonardo, additional, and Raffaelli, Nadia, additional

Published
2011
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34. Novel assay for simultaneous measurement of pyridine mononucleotides synthesizing activities allows dissection of the NAD+ biosynthetic machinery in mammalian cells.

Author

Zamporlini, Federica, Ruggieri, Silverio, Mazzola, Francesca, Amici, Adolfo, Orsomando, Giuseppe, and Raffaelli, Nadia

Subjects
*PYRIDINE nucleotides, *MAMMALIAN cell cycle, *NAD (Coenzyme), *BIOSYNTHESIS, *PHOSPHORIBOSYLTRANSFERASES
Abstract

The redox coenzyme NAD+ is also a rate-limiting co-substrate for several enzymes that consume the molecule, thus rendering its continuous re-synthesis indispensable. NAD+ biosynthesis has emerged as a therapeutic target due to the relevance of NAD+-consuming reactions in complex intracellular signaling networks whose alteration leads to many neurologic and metabolic disorders. Distinct metabolic routes, starting from various precursors, are known to support NAD+ biosynthesis with tissue/cell-specific efficiencies, probably reflecting differential expression of the corresponding rate-limiting enzymes, i.e. nicotinamide phosphoribosyltransferase, quinolinate phosphoribosyltransferase, nicotinate phosphoribosyltransferase and nicotinamide riboside kinase. Understanding the contribution of these enzymes to NAD+ levels depending on the tissue/cell type and metabolic status is necessary for the rational design of therapeutic strategies aimed at modulating NAD+ availability. Here we report a simple, fast and sensitive coupled fluorometric assay that enables simultaneous determination of the four activities in whole-cell extracts and biological fluids. Its application to extracts from various mouse tissues, human cell lines and plasma yielded for the first time an overall picture of the tissue/cell-specific distribution of the activities of the various enzymes. The screening enabled us to gather novel findings, including (a) the presence of quinolinate phosphoribosyltransferase and nicotinamide riboside kinase in all examined tissues/cell lines, indicating that quinolinate and nicotinamide riboside are relevant NAD+ precursors, and (b) the unexpected occurrence of nicotinate phosphoribosyltransferase in human plasma. [ABSTRACT FROM AUTHOR]

Published
2014
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47. Catabolite Inactivation of Bakers'-Yeast Uridine Nucleosidase.

Author

Magni, Giulio, Santarelli, Ivano, Natalini, Paolo, Ruggieri, Silverio, and Vita, Alberto

Subjects
URIDINE, NUCLEOSIDASES, YEAST, ENZYMES, ALCOHOL, CELLS, BIOCHEMISTRY
Abstract

When bakers' yeast cells are grown in culture media containing ethanol instead of glucose, uridine nucleosidase specific activity increased up to 10 times its original value. Addition of glucose to ethanol-grown cells caused a rapid drop of uridine nucleosidase activity. This inactivation could be prevented by the presence of phynylmethylsulfonyl fluoride. Experiments with cycloheximide indicated that both the inactivation and the reappearance of the enzyme activity require protein synthesis. In addition a fraction has been isolated and partially purified from bakers' yeast that is able to inactivate uridine nucleosidase in vitro. The inactivating fraction is not dialyzable, and can be purified using conventional protein purification procedure, suggesting its protein character. The pH optimum of the inactivating activity is around 5 and the factor shows a molecular weight of 75000. Glucose-6-phosphate dehydrogenase, hexokinase, glyceraldehydes-3-phosphate dehydrogenase, cytidine deaminase, cytosine deaminase, 3-phosphoglycerate kinase and glutathione reductase were not inactivated by the preparation. Bakers' yeast boiled crude extract supernatant contained an inhibitor of the inactivating factor. The inactivating protein is endowed also with proteolytic activity and the inhibition exerted byphenylmethylsulfonyl fluoride and by the endogeneous inhibitor indicate that the factor is a protease. [ABSTRACT FROM AUTHOR]

Published
1977
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49. Identification and characterization of YLR328W, the Saccharomyces cerevisiaestructural gene encoding NMN adenylyltransferase. Expression and characterization of the recombinant enzyme

Author

Emanuelli, Monica, Carnevali, Francesco, Lorenzi, Maria, Raffaelli, Nadia, Amici, Adolfo, Ruggieri, Silverio, and Magni, Giulio

Abstract

The enzyme nicotinamide mononucleotide (NMN) adenylyltransferase (EC 2.7.7.1) catalyzes the transfer of the adenylyl moiety of ATP to NMN to form NAD. A new purification procedure for NMN adenylyltransferase from Saccharomyces cerevisiaeprovided sufficient amounts of enzyme for tryptic fragmentation. Through data‐base search a full matching was found between the sequence of tryptic fragments and the sequence of a hypothetical protein encoded by the S. cerevisiaeYLR328W open reading frame (GenBank accession number U20618). The YLR328W gene was isolated, cloned into a T7‐based vector and successfully expressed in Escherichia coliBL21 cells, yielding a high level of NMN adenylyltransferase activity. The purification of recombinant protein, by a two‐step chromatographic procedure, resulted in a single polypeptide of 48 kDa under SDS‐PAGE, in agreement with the molecular mass of the hypothetical protein encoded by YLR328W ORF. The N‐terminal sequence of the purified recombinant NMN adenylyltransferase exactly corresponds to the predicted sequence. Molecular and kinetic properties of recombinant NMN adenylyltransferase are reported and compared with those already known for the enzyme obtained from different sources.

Published
1999
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