Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Erika Zangelmi"'
Autor:
Marco Malatesta, Emanuele Fornasier, Martino Luigi Di Salvo, Angela Tramonti, Erika Zangelmi, Alessio Peracchi, Andrea Secchi, Eugenia Polverini, Gabriele Giachin, Roberto Battistutta, Roberto Contestabile, Riccardo Percudani
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-16 (2024)
Abstract The increasing availability of experimental and computational protein structures entices their use for function prediction. Here we develop an automated procedure to identify enzymes involved in metabolic reactions by assessing substrate con
Externí odkaz:
https://doaj.org/article/14c67f718fbf493085d50d336b285301
Autor:
Erika Zangelmi, Francesca Ruffolo, Tamara Dinhof, Marco Gerdol, Marco Malatesta, Jason P. Chin, Claudio Rivetti, Andrea Secchi, Katharina Pallitsch, Alessio Peracchi
Publikováno v:
iScience, Vol 26, Iss 11, Pp 108108- (2023)
Summary: Phosphonates—compounds containing a direct C–P bond—represent an important source of phosphorus in some environments. The most common natural phosphonate is 2-aminoethylphosphonate (AEP). Many bacteria can break AEP down through specia
Externí odkaz:
https://doaj.org/article/eb026c35632e43a0ad50589384f402e1
Autor:
Francesca Ruffolo, Tamara Dinhof, Leanne Murray, Erika Zangelmi, Jason P. Chin, Katharina Pallitsch, Alessio Peracchi
Publikováno v:
Molecules, Vol 28, Iss 19, p 6863 (2023)
Phosphonates are compounds containing a direct carbon–phosphorus (C–P) bond, which is particularly resistant to chemical and enzymatic degradation. They are environmentally ubiquitous: some of them are produced by microorganisms and invertebrates
Externí odkaz:
https://doaj.org/article/0b2a01c418dd4ffcbf55fa85aab9e37b
Autor:
Francesco Marchesani, Erika Zangelmi, Stefano Bruno, Stefano Bettati, Alessio Peracchi, Barbara Campanini
Publikováno v:
Life, Vol 11, Iss 6, p 485 (2021)
Phosphoserine phosphatase (PSP) catalyzes the final step of de novo L-serine biosynthesis—the hydrolysis of phosphoserine to serine and inorganic phosphate—in humans, bacteria, and plants. In published works, the reaction is typically monitored t
Externí odkaz:
https://doaj.org/article/4959e5de41de4fd28e651f818b2c0632
Autor:
Francesco Marchesani, Erika Zangelmi, Giulia Murtas, Elisa Costanzi, Raheem Ullah, Alessio Peracchi, Stefano Bruno, Loredano Pollegioni, Andrea Mozzarelli, Paola Storici, Barbara Campanini
Publikováno v:
Protein Science. 32
Autor:
Marco Malatesta, Domenico Acquotti, Alessio Peracchi, Toda Stankovic, Katharina Pallitsch, Erika Zangelmi
Publikováno v:
Biochemistry. 60:1214-1225
Phosphonates represent an important source of bioavailable phosphorus in certain environments. Accordingly, many microorganisms (particularly marine bacteria) possess catabolic pathways to degrade ...
Autor:
Francesco Caligiore, Erika Zangelmi, Carola Vetro, Takfarinas Kentache, Joseph P. Dewulf, Maria Veiga-da-Cunha, Emile Van Schaftingen, Guido Bommer, Alessio Peracchi
Publikováno v:
Cellular and Molecular Life Sciences, Vol. 79, no.8, p. 421 (2022)
Transaminases play key roles in central metabolism, transferring the amino group from a donor substrate to an acceptor. These enzymes can often act, with low efficiency, on compounds different from the preferred substrates. To understand what might h
Autor:
Erika, Zangelmi, Toda, Stanković, Marco, Malatesta, Domenico, Acquotti, Katharina, Pallitsch, Alessio, Peracchi
Publikováno v:
Biochemistry
Phosphonates represent an important source of bioavailable phosphorus in certain environments. Accordingly, many microorganisms (particularly marine bacteria) possess catabolic pathways to degrade these molecules. One example is the widespread hydrol
Autor:
Domenico Acquotti, Erika Zangelmi, Alessio Peracchi, Marco Malatesta, Katharina Pallitsch, Toda Stankovic
Phosphonates contain a particularly stable carbon-phosphorus bond, yet a number of microorganisms possess pathways to degrade these molecules and use them as source of phosphorus. One example is the widespread hydrolytic route for the breakdown of 2-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f77595d4e52bc1a4469231689d81f4f3
https://doi.org/10.1101/2020.12.13.422544
https://doi.org/10.1101/2020.12.13.422544
Autor:
Loredano Pollegioni, Alessio Peracchi, Giulia Murtas, Erika Zangelmi, Giorgia Letizia Marcone
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 4231, p 4231 (2021)
Volume 22
Issue 8
International Journal of Molecular Sciences, Vol 22, Iss 4231, p 4231 (2021)
The human enzyme D-3-phosphoglycerate dehydrogenase (hPHGDH) catalyzes the reversible dehydrogenation of 3-phosphoglycerate (3PG) into 3-phosphohydroxypyruvate (PHP) using the NAD+/NADH redox cofactor, the first step in the phosphorylated pathway pro