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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 ...
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 ...
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, ...
On the kinetic and allosteric regulatory properties of the ADP-glucose pyrophosphorylase from Rhodococcus jostii: An approach to evaluate glycogen metabolism in oleaginous bacteria
(Frontiers Research Foundation, 2016-06)
Rhodococcus spp. are oleaginous bacteria that accumulate glycogen during exponential growth. Despite the importance of these microorganisms in biotechnology, little is known about the regulation of carbon and energy storage, ...
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 ...
Regulatory properties of the ADP-glucose pyrophosphorylase from the clostridial Firmicutes member Ruminococcus albus
(American Society for Microbiology, 2018-09)
ADP-glucose pyrophosphorylase from Firmicutes is encoded by two genes (glgC and glgD) leading to a heterotetrameric protein structure, unlike those in other bacterial phyla. The enzymes from two groups of Firmicutes, ...
A colorimetric method for the assay of ADP-glucose pyrophosphorylase
(Academic Press Inc Elsevier Science, 2006-05)
The purpose of the current work was to develop a relatively simple method to assay ADPGlcPPase activity having high sensitivity, accuracy, and reliability. We sought a procedure allowing the assay in both of the reaction ...
ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
(Springer, 2004-12)
In plants, the synthesis of starch occurs by utilizing ADP-glucose as the glucosyl donor for the elongation of α-1,4-glucosidic chains. In photosynthetic bacteria the synthesis of glycogen follows a similar pathway. The ...
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 ...
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 ...