INVESTIGADORES
IGLESIAS Alberto Alvaro
artículos
Título:
The ADP-glucose Pyrophosphorylase from Escherichia coli Comprises Two Tightly-bound Distinct Domains
Autor/es:
C.M. BEJAR; M.A. BALLICORA; D.F. GOMEZ CASATI; A.A. IGLESIAS; J. PREISS
Revista:
FEBS LETTERS
Editorial:
Elsevier
Referencias:
Año: 2004 vol. 573 p. 99 - 104
ISSN:
0014-5793
Resumen:
AbstractComputational 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 yielded an enzyme form as active as the wild type. The only difference from the wild type was a slightly modified affinity for allosteric effectors. The two polypeptides could not be separated by chromatographic procedures. Separate expression of these polypeptides produced inactive unstable forms. All these resultsindicated that the ADP-glucose pyrophosphorylase comprises two domains with a strong interaction between them. That interaction is important for allosteric properties and structuralstability. Keywords: Domain interaction; Glycogen synthesis; ADP-glucose pyrophosphorylase; Regulatory domain
