Studying the phosphoryl transfer mechanism of the E. coli phosphofructokinase-2: from X-ray structure to quantum mechanics/molecular mechanics simulations

Autor: Kirill Zinovjev, Juliana A. Murillo-López, Andrés Caniuguir, Jorge Babul, Rodrigo Recabarren, Jans Alzate-Morales, Julio Caballero, Humberto D'Muniz Pereira, Ricardo Cabrera, Iñaki Tuñón, Richard Charles Garratt

Publikováno v: Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

Phosphofructokinases (Pfks) catalyze the ATP-dependent phosphorylation of fructose-6-phosphate (F6P) and they are regulated in a wide variety of organisms. Although numerous aspects of the kinetics and regulation have been characterized for Pfks, the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92a16ca69a3f012dc9954f6bd8c47262
https://doi.org/10.1039/c9sc00094a

Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+

Autor: Jorge Babul, Andrés Caniuguir, Christian A.M. Wilson, Jaime Andrés Rivas-Pardo, Victoria Guixé

Publikováno v: ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Artículos CONICYT
CONICYT Chile
instacron:CONICYT

The reaction catalyzed by E. coli Pfk-2 presents a dual-cation requirement. In addition to that chelated by the nucleotide substrate, an activating cation is required to obtain full activity of the enzyme. Only Mn 2+ and Mg 2+ can fulfill this role b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80fa27f346335cd29f3c1af38924da99
https://doi.org/10.1016/j.abb.2010.09.020

A ribokinase family conserved monovalent cation binding site enhances the mgatp-induced inhibition in e. Coli phosphofructokinase-2

Autor: Ricardo Cabrera, César A. Ramírez-Sarmiento, Alejandro Toro Blanco, Richard Charles Garratt, Jorge Babul, Andrés Caniuguir, Mauricio Baez, Pablo Villalobos, Humberto M. Pereira, Victoria Guixé

Publikováno v: BIOPHYSICAL JOURNAL
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP

The presence of a regulatory site for monovalent cations that affects the conformation of the MgATP-binding pocket leading to enzyme activation has been demonstrated for ribokinases. This site is selective toward the ionic radius of the monovalent ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5547de028271912c72b49c886258a328

The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP inhibition

Autor: Ricardo, Cabrera, Mauricio, Baez, Humberto M, Pereira, Andrés, Caniuguir, Richard C, Garratt, Jorge, Babul

Publikováno v: The Journal of biological chemistry. 286(7)

Substrate inhibition by ATP is a regulatory feature of the phosphofructokinases isoenzymes from Escherichia coli (Pfk-1 and Pfk-2). Under gluconeogenic conditions, the loss of this regulation in Pfk-2 causes substrate cycling of fructose-6-phosphate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3f473c5c10aa3455c4233130f419643a
https://pubmed.ncbi.nlm.nih.gov/21147773

Role of Cys-295 on subunit interactions and allosteric regulation of phosphofructokinase-2 from Escherichia coli

Autor: Claudio C. Vásquez, Andrés Caniuguir, Mauricio Baez, Victoria Guixé, Jorge Babul, Ricardo Cabrera

Publikováno v: FEBS LETTERS
Artículos CONICYT
CONICYT Chile
instacron:CONICYT

In a previous work, chemical modification of Cys-238 of Escherichia coli Pfk-2 raised concerns on the importance of the dimeric state of Pfk-2 for enzyme activity, whereas modification of Cys-295 impaired the enzymatic activity and the MgATP-induced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dac9f02e105527dffdfad261424ea6a5