Identification of regions critically affecting kinetics and allosteric regulation of the Escherichia coli ADP-glucose pyrophosphorylase by modeling and pentapeptide-scanning mutagenesis

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, we studied the effects of pentapeptide insertions at different positions in the...

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Detalles Bibliográficos
Autores principales: Ballicora, M.A., Erben, E.D., Yazaki, T., Bertolo, A.L., Demonte, A.M., Schmidt, J.R., Aleanzi, M., Bejar, C.M., Figueroa, C.M., Fusari, C.M., Iglesias, A.A., Preiss, J.
Formato: JOUR
Materias:
glucose 1 phosphate adenylyltransferase
leucine
proline
allosterism
article
binding kinetics
catalysis
correlation analysis
enzyme regulation
Escherichia coli
gene insertion
glycogen synthesis
mutagenesis
nonhuman
pentapeptide scanning mutagenesis
priority journal
sequence homology
stop codon
structure activity relation
Adenosine Triphosphate
Amino Acid Sequence
Catalysis
Codon, Terminator
Escherichia coli Proteins
Genes, Bacterial
Glucose-1-Phosphate Adenylyltransferase
Kinetics
Magnesium Chloride
Molecular Sequence Data
Mutagenesis, Insertional
Oligopeptides
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Structural Homology, Protein
Structure-Activity Relationship
Substrate Specificity
Bacteria (microorganisms)
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00219193_v189_n14_p5325_Ballicora
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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