INVESTIGADORES
GOMEZ CASATI Diego Fabian
artículos
Título:
The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly-bound distinct domains
Autor/es:
BEJAR, C.; BALLICORA, M.; DIEGO FABIAN GOMEZ CASATI; IGLESIAS, A.; PREISS, J.
Revista:
FEBS LETTERS
Editorial:
Elsevier
Referencias:
Año: 2004 vol. 573 p. 99 - 104
ISSN:
0014-5793
Resumen:
Computational analysis of ADP-glucose pyrophosphorylases
predicts a fold with two domains. Co-expression of
two polypeptides comprising residues 1323 and 328431 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 results
indicated that the ADP-glucose pyrophosphorylase comprises
two domains with a strong interaction between them. That
interaction is important for allosteric properties and structural
stability.
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 results
indicated that the ADP-glucose pyrophosphorylase comprises
two domains with a strong interaction between them. That
interaction is important for allosteric properties and structural
stability.
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 results
indicated that the ADP-glucose pyrophosphorylase comprises
two domains with a strong interaction between them. That
interaction is important for allosteric properties and structural
stability.