Browsing by Author "Guixé Leguía, Victoria Cristina"
Now showing items 1-20 of 24
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(AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2009-06-24)Some hyperthermophilic archaea use a modified glycolytic pathway that employs an ADP-dependent glucokinase (ADPGK) and an ADP-dependent phosphofructokinase (ADP-PFK) or, in the case of Methanococcus jannaschii, a ...
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(Universidad de ChileCyberDocs, 2010)La enzima piridoxal quinasa (PLK) pertenece a la familia de quinasas sin dominio menor de la superfamilia de la riboquinasa y cataliza la formación de piridoxal-5’-fosfato (PLP) a partir de piridoxal (PL) y de un complejo ...
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(FEBS, 2014)In some archaea, the phosphorylation of glucose and fructose 6-phosphate (fructose 6P) is carried out by enzymes that are specific for either substrate and that use ADP as phosphoryl donor. In the hyperthermophilic ...
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(Elsevier, 2012)In some archaea, glucose degradation proceeds through a modified version of the Embden-Meyerhof pathway where glucose and fructose-6-P phosphorylation is carried out by kinases that use ADP as the phosphoryl donor. Unlike ...
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(Springer, 2013)Pyridoxal 50-phosphate is the active form of vitamin B6 and its deficiency is directly related with several human disorders, which make human pyridoxal kinase (hPLK) an important pharmacologic target. In spite of this, ...
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(Universidad de Chile, 2014)La riboquinasa humana (RK) (E.C. 2.7.15) pertenece a la superfamilia riboquinasa y cataliza la fosforilación de la D-ribosa usando MgATP como cosustrato, produciendo D-ribosa-5-P y ADP. Aunque la D-ribosa participa en ...
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(Wiley & Sons, 2015)The CD73 ectonucleotidase catalyses the hydrolysis of AMP to adenosine, an immunosuppressive molecule. Recent evidence has demonstrated that this ectonucleotidase is up-regulated in T helper type 17 cells when generated in ...
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(2013-06)ADP-dependent glucokinases represent a unique family of kinases that belong to the ribokinase superfamily, being present mainly in hyperthermophilic archaea. For these enzymes there is no agreement about the magnitude of ...
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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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(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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(Elsevier, 2014)In the family of ATP-dependent vitamin kinases, several bifunctional enzymes that phosphorylate hydroxymethyl pyrimidine (HMP) and pyridoxal (PL) have been described besides enzymes specific towards HMP. To determine how ...
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(AMER CHEMICAL SOC,, 2006-04-20)Phosphofructokinase-2 (Pfk-2) from Escherichia coli belongs to the ribokinase family of sugar kinases. One of the signatures observed in amino acid sequences from the ribokinase familiy members is the NXXE motif, which ...
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(Wiley & Sons, 2015)
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(Universidad de Chile, 2023)Las quinasas de vitaminas son fosfotransferasas dependientes de ATP que participan en la biosíntesis de vitamina B1 y B6 fosforilando en general un grupo alcohol primario (R-OH) del sustrato. Dentro de esta familia se han ...
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(ACS Publications, 2015)Enzyme-substrate binding is a dynamic process intimately coupled to protein structural changes, which in turn changes the unfolding energy landscape. By the use of single-molecule force spectroscopy (SMFS), we characterize ...
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(1984)The kinetic mechanisms of Escherichia coli phosphofructokinase-2 (Pfk-2) and of the mutant enzyme Pfk-2* were investigated. Initial velocity studies showed that both enzymes have a sequential kinetic mechanism, indicating ...
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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 ...
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(Springer, 2015)Human ribokinase (RK) is a member of the ribokinase family, and is the first enzyme responsible for D-ribose metabolism, since D-ribose must first be converted into D-ribose-5-phosphate to be further metabolized and ...
