Search results for: Francesca Cutruzzolà

Items from 1 to 20 out of 45 results

article

Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

Sharon Spizzichino, Dalila Boi, Giovanna Boumis, Roberta Lucchi, more

The FEBS Journal > 289 > 6 > 1625 - 1649

De novo thymidylate synthesis is a crucial pathway for normal and cancer cells. Deoxythymidine monophosphate (dTMP) is synthesized by the combined action of three enzymes: serine hydroxymethyltransferase (SHMT1), dihydrofolate reductase (DHFR) and thymidylate synthase (TYMS), with the latter two being targets of widely used chemotherapeutics such as antifolates and 5‐fluorouracil. These proteins translocate...

article

Crystal structure of Aspergillus fumigatus AroH, an aromatic amino acid aminotransferase

Sharon Spizzichino, Gioena Pampalone, Mirco Dindo, Agostino Bruno, more

Proteins: Structure, Function, and Bioinformatics > 90 > 2 > 435 - 442

Aspergillus fumigatus is a saprophytic ubiquitous fungus whose spores can trigger reactions such as allergic bronchopulmonary aspergillosis or the fatal invasive pulmonary aspergillosis. To survive in the lungs, the fungus must adapt to a hypoxic and nutritionally restrictive environment, exploiting the limited availability of aromatic amino acids (AAAs) in the best possible way, as mammals do not...

article

Basic and applied science at the time of COVID‐19

Governing Council of the Italian Society of Biochemistry and Molecular Biology, Board of the Italian Professors of Biochemistry, Martino Bolognesi, Mauro Magnani, more

FEBS Letters > 594 > 18 > 2933 - 2934

article

R180T variant of δ‐ornithine aminotransferase associated with gyrate atrophy: biochemical, computational, X‐ray and NMR studies provide insight into its catalytic features

Riccardo Montioli, Alessandro Paiardini, Giorgio Giardina, Serena Zanzoni, more

The FEBS Journal > 286 > 14 > 2787 - 2798

Among the over 50 gyrate atrophy‐causing mutations of ornithine δ‐aminotransferase (OAT), the R180T involves an active site residue located at the dimer interface, which in the crystal structure of OAT complexed with 5‐fluoromethylornithine engages a salt bridge with the α‐carboxylate of the substrate analogue. Starting from the previous finding that no transaminase activity was detected in CHO‐K...

article

Insights into the GTP‐dependent allosteric control of c‐di‐GMP hydrolysis from the crystal structure of PA0575 protein from Pseudomonas aeruginosa

Federico Mantoni, Alessandro Paiardini, Paolo Brunotti, Cecilia D'Angelo, more

The FEBS Journal > 285 > 20 > 3815 - 3834

Bis‐(3′‑5′)‐cyclic diguanylic acid (c‑di‑GMP) belongs to the class of cyclic dinucleotides, key carriers of cellular information in prokaryotic and eukaryotic signal transduction pathways. In bacteria, the intracellular levels of c‐di‐GMP and their complex physiological outputs are dynamically regulated by environmental and internal stimuli, which control the antagonistic activities of diguanylate...

article

The catalytic activity of serine hydroxymethyltransferase is essential for de novo nuclear dTMP synthesis in lung cancer cells

Giorgio Giardina, Alessio Paone, Angela Tramonti, Roberta Lucchi, more

The FEBS Journal > 285 > 17 > 3238 - 3253

Cancer cells reprogramme one‐carbon metabolism (OCM) to sustain growth and proliferation. Depending on cell demands, serine hydroxymethyltransferase (SHMT) dynamically changes the fluxes of OCM by reversibly converting serine and tetrahydrofolate (THF) into 5,10‐methylene‐THF and glycine. SHMT is a tetrameric enzyme that mainly exists in three isoforms; two localize in the cytosol (SHMT1/SHMT2α)...

article

Differential inhibitory effect of a pyrazolopyran compound on human serine hydroxymethyltransferase-amino acid complexes

Angela Tramonti, Alessandro Paiardini, Alessio Paone, Amani Bouzidi, more

Archives of Biochemistry and Biophysics > 2018 > 653 > C > 71-79

Serine hydroxymethyltransferase (SHMT) is a pivotal enzyme in one-carbon metabolism that catalyses the reversible conversion of serine and tetrahydrofolate into glycine and methylenetetrahydrofolate. It exists in cytosolic (SHMT1) and mitochondrial (SHMT2) isoforms. Research on one-carbon metabolism in cancer cell lines has shown that SHMT1 preferentially catalyses serine synthesis, whereas in mitochondria...

article

Differential 3-bromopyruvate inhibition of cytosolic and mitochondrial human serine hydroxymethyltransferase isoforms, key enzymes in cancer metabolic reprogramming

Alessandro Paiardini, Angela Tramonti, Doug Schirch, Giulia Guiducci, more

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics > 2016 > 1864 > 11 > 1506-1517

The cytosolic and mitochondrial isoforms of serine hydroxymethyltransferase (SHMT1 and SHMT2, respectively) are well-recognized targets of cancer research, since their activity is critical for purine and pyrimidine biosynthesis and because of their prominent role in the metabolic reprogramming of cancer cells. Here we show that 3-bromopyruvate (3BP), a potent novel anti-tumour agent believed to function...

article

How pyridoxal 5′‐phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state

Giorgio Giardina, Paolo Brunotti, Alessio Fiascarelli, Alessandra Cicalini, more

The FEBS Journal > 282 > 7 > 1225 - 1241

Adaptive metabolic reprogramming gives cancer cells a proliferative advantage. Tumour cells extensively use glycolysis to sustain anabolism and produce serine, which not only refuels the one‐carbon units necessary for the synthesis of nucleotide precursors and for DNA methylation, but also affects the cellular redox homeostasis. Given its central role in serine metabolism, serine hydroxymethyltransferase...

article

Serine and glycine metabolism in cancer

Ivano Amelio, Francesca Cutruzzolá, Alexey Antonov, Massimiliano Agostini, more

Trends in Biochemical Sciences > 2014 > 39 > 4 > 191-198

Serine and glycine are biosynthetically linked, and together provide the essential precursors for the synthesis of proteins, nucleic acids, and lipids that are crucial to cancer cell growth. Moreover, serine/glycine biosynthesis also affects cellular antioxidative capacity, thus supporting tumour homeostasis. A crucial contribution of serine/glycine to cellular metabolism is through the glycine cleavage...

article

Distal–proximal crosstalk in the heme binding pocket of the NO sensor DNR

Francesca Cutruzzolà, Alessandro Arcovito, Giorgio Giardina, Stefano della Longa, more

BioMetals > 2014 > 27 > 4 > 763-773

In the opportunistic pathogen Pseudomonas aeruginosa the denitrification process is triggered by nitric oxide (NO) and plays a crucial role for the survival in chronic infection sites as a microaerobic–anaerobic biofilm. This respiratory pathway is transcriptionally induced by DNR, an heme-based gas sensor which positively responds to NO. Molecular details of the NO sensing mechanism employed by DNR...

article

The immunosuppressive drug azathioprine inhibits biosynthesis of the bacterial signal molecule cyclic-di-GMP by interfering with intracellular nucleotide pool availability

Davide Antoniani, Elio Rossi, Serena Rinaldo, Paola Bocci, more

Applied Microbiology and Biotechnology > 2013 > 97 > 16 > 7325-7336

In Gram-negative bacteria, production of the signal molecule c-di-GMP by diguanylate cyclases (DGCs) is a key trigger for biofilm formation, which, in turn, is often required for the development of chronic bacterial infections. Thus, DGCs represent interesting targets for new chemotherapeutic drugs with anti-biofilm activity. We searched for inhibitors of the WspR protein, a Pseudomonas aeruginosa...

article

Nitric oxide synthesis by bacterial cytochrome cd1 nitrite reductases

Francesca Cutruzzolà

Nitric Oxide > 2012 > 27 > Supplement > S10

Cytochrome cd ₁ nitrite reductase (cd ₁ NIR) is a haem-containing enzyme responsible for the reduction of nitrite into nitric oxide (NO), a key step in the bacterial anaerobic respiratory process of denitrification. The active site of cytochrome cd ₁ contains the unique d ₁ -haem cofactor, from which NO must be released. In general, reduced haems bind NO tightly relative...

article

In silico and in vitro validation of serine hydroxymethyltransferase as a chemotherapeutic target of the antifolate drug pemetrexed

Frederick Daidone, Rita Florio, Serena Rinaldo, Roberto Contestabile, more

European Journal of Medicinal Chemistry > 2011 > 46 > 5 > 1616-1621

Serine hydroxymethyltransferase (SHMT), a ubiquitous representative of the family of fold-type I, pyridoxal 5′-phosphate (PLP) dependent enzymes, catalyzes the reversible conversion of tetrahydrofolate (H ₄ PteGlu) and serine to 5,10-CH ₂ –H ₄ PteGlu and glycine. Together with thymidylate synthase (TS) and dihydrofolate reductase (DHFR), SHMT participates to the thymidylate...

article

Dynamic Hydrogen-Bonding Network in the Distal Pocket of the Nitrosyl Complex of Pseudomonas aeruginosa cd ₁ Nitrite Reductase

Marina Radoul, Dmytro Bykov, Serena Rinaldo, Francesca Cutruzzolà, more

Journal of the American Chemical Society > 2011 > 133 > 9 > 3043 - 3055

article

Heme d ₁ Nitrosyl Complex of cd ₁ Nitrite Reductase Studied by High-Field-Pulse Electron Paramagnetic Resonance Spectroscopy

Marina Radoul, Fabio Centola, Serena Rinaldo, Francesca Cutruzzolà, more

Inorganic Chemistry > 2009 > 48 > 9 > 3913 - 3915

article

Intramolecular Electron Transfer in Pseudomonas aeruginosa cd1 Nitrite Reductase: Thermodynamics and Kinetics

Ole Farver, Maurizio Brunori, Francesca Cutruzzolà, Serena Rinaldo, more

Biophysical Journal > 2009 > 96 > 7 > 2849-2856

The cd₁ nitrite reductases, which catalyze the reduction of nitrite to nitric oxide, are homodimers of 60 kDa subunits, each containing one heme-c and one heme-d₁. Heme-c is the electron entry site, whereas heme-d₁ constitutes the catalytic center. The 3D structure of Pseudomonas aeruginosa nitrite reductase has been determined in both fully oxidized and reduced states. Intramolecular electron transfer...

article

NO sensing in Pseudomonas aeruginosa: Structure of the Transcriptional Regulator DNR

Giorgio Giardina, Serena Rinaldo, Kenneth A. Johnson, Adele Di Matteo, more

Journal of Molecular Biology > 2008 > 378 > 5 > 1002-1015

All denitrifying bacteria can keep the steady-state concentrations of nitrite and nitric oxide (NO) below cytotoxic levels, controlling the expression of the denitrification gene clusters by redox signaling, mainly through transcriptional regulators belonging either to the DNR (dissimilative nitrate respiration regulator) or to the NnrR (nitrite and nitric oxide reductase regulator) subgroups of the...

article

Tyrosine as a redox-active center in electron transfer to ferryl heme in globins

Brandon J. Reeder, Francesca Cutruzzola, Maria Giulia Bigotti, Robert C. Hider, more

Free Radical Biology and Medicine > 2008 > 44 > 3 > 274-283

A wide range of organic reductants, including many iron chelators, reduce ferryl myoglobin to its ferric states in exponential time courses whose rate constants display double hyperbolic dependencies on the reductant concentration. This concentration dependence is consistent with a mechanism in which electron transfer to the heme takes place at two independent sites where reductants appear to bind...

article

Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase

Serena Rinaldo, Maurizio Brunori, Francesca Cutruzzolà

Biochemical and Biophysical Research Communications > 2007 > 363 > 3 > 662-666

Nitrite reductase (cd ₁ NIR) from Pseudomonas aeruginosa, which catalyses the reduction of nitrite to nitric oxide (NO), contains a c-heme as the electron acceptor and a d ₁ -heme where catalysis occurs. Reduction involves binding of nitrite to the reduced d ₁ -heme, followed by dehydration to yield NO; release of NO and re-reduction of the enzyme close the cycle. Since NO...

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INFONA - science communication portal

Search results for: Francesca Cutruzzolà

Cytosolic localization and in vitro assembly of human de novo thymidylate synthesis complex

Crystal structure of Aspergillus fumigatus AroH, an aromatic amino acid aminotransferase

Basic and applied science at the time of COVID‐19

R180T variant of δ‐ornithine aminotransferase associated with gyrate atrophy: biochemical, computational, X‐ray and NMR studies provide insight into its catalytic features

Insights into the GTP‐dependent allosteric control of c‐di‐GMP hydrolysis from the crystal structure of PA0575 protein from Pseudomonas aeruginosa

The catalytic activity of serine hydroxymethyltransferase is essential for de novo nuclear dTMP synthesis in lung cancer cells

Differential inhibitory effect of a pyrazolopyran compound on human serine hydroxymethyltransferase-amino acid complexes

Differential 3-bromopyruvate inhibition of cytosolic and mitochondrial human serine hydroxymethyltransferase isoforms, key enzymes in cancer metabolic reprogramming

How pyridoxal 5′‐phosphate differentially regulates human cytosolic and mitochondrial serine hydroxymethyltransferase oligomeric state

Serine and glycine metabolism in cancer

Distal–proximal crosstalk in the heme binding pocket of the NO sensor DNR

The immunosuppressive drug azathioprine inhibits biosynthesis of the bacterial signal molecule cyclic-di-GMP by interfering with intracellular nucleotide pool availability

Nitric oxide synthesis by bacterial cytochrome cd1 nitrite reductases

In silico and in vitro validation of serine hydroxymethyltransferase as a chemotherapeutic target of the antifolate drug pemetrexed

Dynamic Hydrogen-Bonding Network in the Distal Pocket of the Nitrosyl Complex of Pseudomonas aeruginosa cd ₁ Nitrite Reductase

Heme d ₁ Nitrosyl Complex of cd ₁ Nitrite Reductase Studied by High-Field-Pulse Electron Paramagnetic Resonance Spectroscopy

Intramolecular Electron Transfer in Pseudomonas aeruginosa cd1 Nitrite Reductase: Thermodynamics and Kinetics

NO sensing in Pseudomonas aeruginosa: Structure of the Transcriptional Regulator DNR

Tyrosine as a redox-active center in electron transfer to ferryl heme in globins

Nitrite controls the release of nitric oxide in Pseudomonas aeruginosa cd1 nitrite reductase

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