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Unraveling the activation mechanism of the potato tuber ADP-glucose pyrophosphorylaseOstreococcus tauri ADP-glucose pyrophosphorylase reveals alternative paths for the evolution of subunit roles.A novel dual allosteric activation mechanism of Escherichia coli ADP-glucose pyrophosphorylase: the role of pyruvateFunctional demonstrations of starch binding domains present in Ostreococcus tauri starch synthases isoforms.The Crystal Structure of Nitrosomonas europaea Sucrose Synthase Reveals Critical Conformational Changes and Insights into Sucrose Metabolism in Prokaryotes.Monofluorophosphate Blocks Internal Polysaccharide Synthesis in Streptococcus mutansInsights into glycogen metabolism in chemolithoautotrophic bacteria from distinctive kinetic and regulatory properties of ADP-glucose pyrophosphorylase from Nitrosomonas europaea.Aspartate residue 142 is important for catalysis by ADP-glucose pyrophosphorylase from Escherichia coli.Conserved residues of the Pro103-Arg115 loop are involved in triggering the allosteric response of the Escherichia coli ADP-glucose pyrophosphorylase.Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesisA Chimeric UDP-glucose pyrophosphorylase produced by protein engineering exhibits sensitivity to allosteric regulators.Allosteric Control of Substrate Specificity of the Escherichia coli ADP-Glucose Pyrophosphorylase.On the Ancestral UDP-Glucose Pyrophosphorylase Activity of GalF from Escherichia coli.The ADP-glucose pyrophosphorylase from Streptococcus mutans provides evidence for the regulation of polysaccharide biosynthesis in Firmicutes.ADP-glucose pyrophosphorylase from potato tuber: site-directed mutagenesis of homologous aspartic acid residues in the small and large subunits.The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme.An assay for adenosine 5'-diphosphate (ADP)-glucose pyrophosphorylase that measures the synthesis of radioactive ADP-glucose with glycogen synthase.The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases.Two Arabidopsis ADP-glucose pyrophosphorylase large subunits (APL1 and APL2) are catalytic.Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase.Adenosine 5'-diphosphate-glucose pyrophosphorylase from potato tuber. Significance of the N terminus of the small subunit for catalytic properties and heat stability.Molecular architecture of the glucose 1-phosphate site in ADP-glucose pyrophosphorylases.On the stability of nucleoside diphosphate glucose metabolites: implications for studies of plant carbohydrate metabolism.Identification and characterization of a novel starch branching enzyme from the picoalgae Ostreococcus tauri.Identification of a novel starch synthase III from the picoalgae Ostreococcus tauri.Practical spectrophotometric assay for the dapE-encoded N-succinyl-L,L-diaminopimelic acid desuccinylase, a potential antibiotic target.Understanding the allosteric trigger for the fructose-1,6-bisphosphate regulation of the ADP-glucose pyrophosphorylase from Escherichia coli.The ADP-glucose binding site of the Escherichia coli glycogen synthase.Chloroplast fructose-1,6-bisphosphatase: modification of non-covalent interactions promote the activation by chimeric Escherichia coli thioredoxins.Enhancement of the reductive activation of chloroplast fructose-1,6-bisphosphatase by modulators and protein perturbantsActivation of the potato tuber ADP-glucose pyrophosphorylase by thioredoxinADP-Glucose pyrophosphorylase from potato tubers. Site-directed mutagenesis studies of the regulatory sitesMechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylaseHeat stability of the potato tuber ADP-glucose pyrophosphorylase: role of Cys residue 12 in the small subunitRegulatory properties of potato-Arabidopsis hybrid ADP-glucose pyrophosphorylaseThe ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domainsADP-Glucose Pyrophosphorylase: A Regulatory Enzyme for Plant Starch SynthesisMutagenesis of the glucose-1-phosphate-binding site of potato tuber ADP-glucose pyrophosphorylase
P50
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P50
description
researcher ORCID ID = 0000-0002-5324-0724
@en
wetenschapper
@nl
name
Miguel A Ballicora
@ast
Miguel A Ballicora
@en
Miguel A Ballicora
@es
Miguel A Ballicora
@nl
type
label
Miguel A Ballicora
@ast
Miguel A Ballicora
@en
Miguel A Ballicora
@es
Miguel A Ballicora
@nl
prefLabel
Miguel A Ballicora
@ast
Miguel A Ballicora
@en
Miguel A Ballicora
@es
Miguel A Ballicora
@nl
P106
P21
P31
P496
0000-0002-5324-0724