Publications by authors named "Alicia Vega-Segura"

Article Synopsis
  • - Eukarya pyruvate kinases differ from bacterial ones by having glutamate at position 117, affecting their dependence on potassium; those with E117 require K (K-dependent), while those with K117 do not (K-independent).
  • - The study explores how specific amino acid residues influence the function of K-independent pyruvate kinases, particularly highlighting the roles of residues 117 and 120 in enzyme conformation and activity.
  • - Results indicate that K-independent enzymes may use distinct mechanisms for catalysis compared to K-dependent ones, with K117 influencing the enzyme's structure and substrate interaction significantly.
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Phosphate metabolism was studied to determine whether polyphosphate (polyP) pools play a role in the enhanced resistance against Cd and metal-removal capacity of Cd-preadapted (CdPA) . Polyphosphate kinase (PPK), exopolyphosphatase (PPX) and phosphate transporter transcript levels and their activities increased in CdPA cells compared to control (Cnt) cells. K inhibited recombinant Ma-PPK and activated Ma-PPX, whereas divalent cations activated both enzymes.

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Living organisms are subject to stress, and among these stressors, heavy metals exposure triggers accumulation of sulfur metabolites. Among these metabolites, glutathione and phytochelatins are found in several organisms, such as Euglena gracilis. Pre-exposing E.

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Some kinetic and thermodynamic properties of the plasma membrane adenylyl cyclase (AC) from the protist Euglena gracilis were examined. The AC kinetics for Mg-ATP was hyperbolic with a K(m) value of 0.33-0.

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Adenylate cyclases (ACs) catalyze the formation of 3',5'-cyclic AMP (cAMP) from ATP. A novel AC-encoding gene, cyaC, was isolated from Rhizobium etli by phenotypic complementation of an Escherichia coli cya mutant. The functionality of the cyaC gene was corroborated by its ability to restore cAMP accumulation in an E.

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