Divalent metal cation requirements of phosphofructokinase-2 from E. coli. Evidence for a high affinity binding site for Mn2+-Reference-Cited by-同舟云学术

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

Published:2011-01 Issue:1 Volume:505 Page:60-66
ISSN:0003-9861
Container-title:Archives of Biochemistry and Biophysics
language:en
Short-container-title:Archives of Biochemistry and Biophysics

Author:

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

Funder

Fondo Nacional de Desarrollo Científico y Tecnológico

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference26 articles.

1. The ADP-dependent sugar kinase family: Kinetic and evolutionary aspects

2. Enzyme-Catalyzed Phosphoryl Transfer Reactions

3. An equivalent metal ion in one- and two-metal-ion catalysis

4. NMR Studies of the Mechanism of Action and Regulation of Protein Kinase

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1. Quantitative assessment of methane bioconversion based on kinetics and bioenergetics;Bioresource Technology;2024-10

2. Studying the phosphoryl transfer mechanism of the E. coli phosphofructokinase-2: from X-ray structure to quantum mechanics/molecular mechanics simulations;Chemical Science;2019

3. 6-Phosphofructokinase and ribulose-5-phosphate 3-epimerase in methylotrophic Bacillus methanolicus ribulose monophosphate cycle;Applied Microbiology and Biotechnology;2017-02-17

4. Dissecting the functional roles of the conserved NXXE and HXE motifs of the ADP-dependent glucokinase fromThermococcus litoralis;FEBS Letters;2015-09-30

5. Role of monovalent and divalent metal cations in human ribokinase catalysis and regulation;BioMetals;2015-03-08

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