Browsing by Author "201-0281205"
Now showing items 1-20 of 30
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(Portland Press Ltd, 1997)Strains of Escherichia coli bearing different forms of phosphofructokinase were used to assess the occurrence of futile cycling in cell resuspensions supplied with glycerol as gluconeogenic carbon source. A model was used ...
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A new method of assessing rates of the futile cycle during glycolytic and gluconeogenic metabolism (1995)A method for assessing rates of the futile cycle is presented, and it is illustrated in vitro. Glycolytic- and gluconeogenic-type cycles are simulated for the reactions catalyzed by phosphofructokinase (EC 2.7.1.11) and ...
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(1978)The proline peptide isomerization model of protein folding predicts that the fraction of denatured polypeptide chains which rapidly fold should be quantitatively related to the numbers of cis and trans proline residues in ...
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Biophysical and evolutionary aspects of domain swapping in the forkhead domain of human FoxP protein (Cell Press, 2017-02-03)
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(BLACKWELL, 2006-09)Escherichia coli contains two phosphofructokinases, Pfk-1 and Pfk-2, which belong to unrelated protein families. In addition to catalytic function, the enzymes have converged in showing substrate inhibition by the nucleotide ...
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(ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD, 2008-08-22)Phosphofructokinase-1 and -2 (Pfk-1 and Pfk-2, respectively) from Escherichia coli belong to different homologous superfamilies. However, in spite of the lack of a common ancestor, they share the ability to catalyze ...
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(Elsevier, 2011)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 Mn2+ and ...
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(2012)Folding studies have been focused mainly on small, single-domain proteins or isolated single domains of larger proteins. However, most of the proteins present in biological systems are composed of multiple domains, and to ...
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(2011)Phosphofructokinase-2 is a 66 kD homodimer whose subunits are associated by means of a bimolecular domain, the β-clasp, which is linked to the larger portion of each subunit by a reentrant chain topology. To investigate ...
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(1993)We present a comparative study of Escherichia coli with normal and increased amounts of fructose-1,6-bisphosphate aldolase. Most experiments employed a resting cell system involving a high cell density (so as to obtain the ...
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(1988)The aggregation states of Escherichia coli phosphofructokinase 2 (Pfk-2) and of a mutant enzyme (Pfk-2*) altered in the inhibitory allosteric site for MgATP were measured in the presence and in the absence of substrates ...
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(Academic Press Inc., 2017)© 2016 Elsevier Inc.DNA staining in gels has historically been carried out using silver staining and fluorescent dyes like ethidium bromide and SYBR Green I (SGI). Using fluorescent dyes allows recovery of the analyte, but ...
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(2013)Phosphofructokinase-2 is a dimeric enzyme that undergoes cold denaturation following a highly cooperative N2 2I mechanism with dimer dissociation and formation of an expanded monomeric intermediate. Here, we use intrinsic ...
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(1972)Absorption spectral, circular dichroic spectral, and viscosity measurements indicate that the compact low-spin conformation characteristic of native cytochrome c is quantitatively recovered from its extended high-spin ...
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(Elsevier B.V., 2016)© 2016 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM) We have proposed an allosteric ATP inhibition mechanism of Pfk-2 determining the structure of different forms of the enzyme together ...
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(ELSEVIER SCIENCE BV, 2009-05-22)Escherichia coli phosphofructokinase-2 (Pfk-2) is a homodimer whose subunits consist of a large domain and an additional b-sheet that provides the interfacial contacts between the subunits, creating a b-barrel flattened-like ...
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(ELSEVIER SCIENCE BV, 2005-04-25)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 ...
