Regulatory network of the allosteric ATP inhibition of E. coli phosphofructokinase-2 studied by hybrid dimers
Author:
Funder
FONDECYT
Conicyt, Chile (JB)
Conicyt doctoral fellowship
Publisher
Elsevier BV
Subject
General Medicine,Biochemistry
Reference20 articles.
1. Phosphofructokinases from Escherichia coli. Purification and characterization of the nonallosteric isozyme;Babul;J. Biol. Chem.,1978
2. The crystal complex of phosphofructokinase-2 of Escherichia coli with fructose-6-phosphate: kinetic and structural analysis of the allosteric ATP inhibition;Cabrera;J. Biol. Chem.,2011
3. Crystallographic structure of phosphofructokinase-2 from Escherichia coli in complex with two ATP molecules. Implications for substrate inhibition;Cabrera;J. Mol. Biol.,2008
4. Regeneration of active enzyme by formation of hybrids from inactive derivatives: implications for active sites shared between polypeptide chains of aspartate transcarbamoylase;Robey;Proc. Natl. Acad. Sci. U. S. A.,1985
5. Disentangling the web of allosteric communication in a homotetramer: heterotropic inhibition of phosphofructokinase from Bacillus stearothermophilus†;Ortigosa;Biochemistry.,2003
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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
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