Zobrazeno 1 - 6 of 6 pro vyhledávání: '"Iralis López-Villamizar"'
1
Akademický článek
Substrate Specificity of Chimeric Enzymes Formed by Interchange of the Catalytic and Specificity Domains of the 5′-Nucleotidase UshA and the 3′-Nucleotidase CpdB
Autor: Alicia Cabezas, Iralis López-Villamizar, María Jesús Costas, José Carlos Cameselle, João Meireles Ribeiro
Publikováno v: Molecules, Vol 26, Iss 8, p 2307 (2021)
The 5′-nucleotidase UshA and the 3′-nucleotidase CpdB from Escherichia coli are broad-specificity phosphohydrolases with similar two-domain structures. Their N-terminal domains (UshA_Ndom and CpdB_Ndom) contain the catalytic site, and their C-ter
Externí odkaz: https://doaj.org/article/20a7d6a41a58485e9ede8388b42a0d0c
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2
Akademický článek
The Characterization of Escherichia coli CpdB as a Recombinant Protein Reveals that, besides Having the Expected 3´-Nucleotidase and 2´,3´-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active as Cyclic Dinucleotide Phosphodiesterase.
Autor: Iralis López-Villamizar, Alicia Cabezas, Rosa María Pinto, José Canales, João Meireles Ribeiro, José Carlos Cameselle, María Jesús Costas
Publikováno v: PLoS ONE, Vol 11, Iss 6, p e0157308 (2016)
Endogenous cyclic diadenylate phosphodiesterase activity was accidentally detected in lysates of Escherichia coli BL21. Since this kind of activity is uncommon in Gram-negative bacteria, its identification was undertaken. After partial purification a
Externí odkaz: https://doaj.org/article/ab285a3e43394d8289b1ec4f464a71c6
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3
Akademický článek
Molecular bases of catalysis and ADP-ribose preference of human Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase and conversion by mutagenesis to a preferential cyclic ADP-ribose phosphohydrolase.
Autor: Alicia Cabezas, João Meireles Ribeiro, Joaquim Rui Rodrigues, Iralis López-Villamizar, Ascensión Fernández, José Canales, Rosa María Pinto, María Jesús Costas, José Carlos Cameselle
Publikováno v: PLoS ONE, Vol 10, Iss 2, p e0118680 (2015)
Among metallo-dependent phosphatases, ADP-ribose/CDP-alcohol diphosphatases form a protein family (ADPRibase-Mn-like) mainly restricted, in eukaryotes, to vertebrates and plants, with preferential expression, at least in rodents, in immune cells. Rat
Externí odkaz: https://doaj.org/article/f0b9e68d337d46949f2feecc9dc67516
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4
Molecular Dissection of Escherichia coli CpdB: Roles of the N Domain in Catalysis and Phosphate Inhibition, and of the C Domain in Substrate Specificity and Adenosine Inhibition
Autor: Joaquim Rui Rodrigues, María Jesús Costas, José Carlos Cameselle, Alicia Cabezas, Iralis López-Villamizar, José Canales, João Meireles Ribeiro, Rosa María Pinto
Publikováno v: International Journal of Molecular Sciences
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 1977, p 1977 (2021)
CpdB is a 3′-nucleotidase/2′3′-cyclic nucleotide phosphodiesterase, active also with reasonable efficiency on cyclic dinucleotides like c-di-AMP (3′,5′-cyclic diadenosine monophosphate) and c-di-GMP (3′,5′-cyclic diadenosine monophospha
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::686a63b1d444b03152a49fc2a92b492a
http://europepmc.org/articles/PMC7922932
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5
Molecular Bases of Catalysis and ADP-Ribose Preference of Human Mn2+-Dependent ADP-Ribose/CDP-Alcohol Diphosphatase and Conversion by Mutagenesis to a Preferential Cyclic ADP-Ribose Phosphohydrolase
Autor: João Meireles Ribeiro, Joaquim Rui Rodrigues, José Canales, Alicia Cabezas, José Carlos Cameselle, Ascensión Fernández, Iralis López-Villamizar, María Jesús Costas, Rosa María Pinto
Publikováno v: Repositório Científico de Acesso Aberto de Portugal
Repositório Científico de Acesso Aberto de Portugal (RCAAP)
instacron:RCAAP
PLoS ONE
PLoS ONE, Vol 10, Iss 2, p e0118680 (2015)
Among metallo-dependent phosphatases, ADP-ribose/CDP-alcohol diphosphatases form a protein family (ADPRibase-Mn-like) mainly restricted, in eukaryotes, to vertebrates and plants, with preferential expression, at least in rodents, in immune cells. Rat
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::846463ce1cbdf00ef715638c9540ddc8
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6
The Characterization of Escherichia coli CpdB as a Recombinant Protein Reveals that, besides Having the Expected 3´-Nucleotidase and 2´,3´-Cyclic Mononucleotide Phosphodiesterase Activities, It Is Also Active as Cyclic Dinucleotide Phosphodiesterase
Autor: María Jesús Costas, Rosa María Pinto, Iralis López-Villamizar, João Meireles Ribeiro, José Canales, José Carlos Cameselle, Alicia Cabezas
Publikováno v: PLoS ONE
PLoS ONE, Vol 11, Iss 6, p e0157308 (2016)
Endogenous cyclic diadenylate phosphodiesterase activity was accidentally detected in lysates of Escherichia coli BL21. Since this kind of activity is uncommon in Gram-negative bacteria, its identification was undertaken. After partial purification a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4732739802028cd575a20ee637083052
https://doi.org/10.1371/journal.pone.0157308
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