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The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains
(Elsevier Science, 2004-08-27)
Computational analysis of ADP-glucose pyrophosphorylases predicts a fold with two domains. Co-expression of two polypeptides comprising residues 1-323 and 328-431 from the Escherichia coli ADP-glucose pyrophosphorylase ...
A Chimeric UDP-Glucose Pyrophosphorylase Produced by Protein Engineering Exhibits Sensitivity to Allosteric Regulators
(Molecular Diversity Preservation International, 2013-05)
In bacteria, glycogen or oligosaccharide accumulation involves glucose-1-phosphate partitioning into either ADP-glucose (ADP-Glc) or UDP-Glc. Their respective synthesis is catalyzed by allosterically regulated ADP-Glc ...
ADP-glucose Pyrophosphorylase; a Regulatory Enzyme for Bacterial Glycogen Synthesis
(American Society for Microbiology, 2003-12)
ADP-Glucose Pyrophosphorylase, a Regulatory Enzyme forBacterial Glycogen SynthesisMiguel A. Ballicora,1 Alberto A. Iglesias,2 and Jack Preiss1*Department of Biochemistry and Molecular Biology, Michigan State University, ...
An assay for adenosine 5′-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase
(Academic Press Inc Elsevier Science, 2004-01)
Adenosine 5′-diphosphate (ADP)-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the conversion of glucose 1-phosphate and adenosine 5′-triphosphate to ADP-glucose and pyrophosphate. We present a radioactive assay of ...
Characterization of recombinant UDP- and ADP-glucose pyrophosphorylases and glycogen synthase to elucidate glucose-1-phosphate partitioning into oligo- and polysaccharides in streptomyces coelicolor
(American Society for Microbiology, 2012-03)
Streptomyces coelicolor exhibits a major secondary metabolism, deriving important amounts of glucose to synthesize pigmented antibiotics. Understanding the pathways occurring in the bacterium with respect to synthesis of ...
Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase
(Oxford University Press, 2006-02)
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the regulatory step in the pathway for synthesis of bacterial glycogen and starch in plants. ADP-Glc PPases from cyanobacteria (homotetramer) and from potato (Solanum ...
Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis
(American Society for Microbiology, 2007-07)
ADP-glucose pyrophosphorylase (ADP-Glc PPase) is the enzyme responsible for the regulation of bacterial glycogen synthesis. To perform a structure-function relationship study of the Escherichia coli ADP-Glc PPase enzyme, ...
The ADP-glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes
(Wiley, 2013-10)
Streptococcus mutans is the leading cause of dental caries worldwide. The bacterium accumulates a glycogen-like internal polysaccharide, which mainly contributes to its carionegic capacity. S. mutans has two genes (glgC ...
Resurrecting the regulatory properties of the ostreococcus tauri ADP-glucose pyrophosphorylase large subunit
(Frontiers Media S.A., 2018-10)
ADP-glucose pyrophosphorylase (ADP-Glc PPase) catalyzes the first committed step for the synthesis of glycogen in cyanobacteria and starch in green algae and plants. The enzyme from cyanobacteria is homotetrameric (α4), ...
Caracterización cinética, regulatoria y estructural de enzimas involucradas en el metabolismo de polisacáridos de reserva en bacterias
(2013-03-12)
La acumulación de glucógeno ha sido bien caracterizada en bacterias Gram negativas. Se ha evidenciado que ADP-glucosa pirofosforilasa (ADP-GlcPPasa) cataliza el paso de la síntesis del donante de glicosilo para la elongación ...