PMID:15327982

Citation	Bejar, CM, Ballicora, MA, Gómez-Casati, DF, Iglesias, AA and Preiss, J (2004) The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains. FEBS Lett. 573:99-104
Abstract	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 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.
Links	PubMed Online version:10.1016/j.febslet.2004.07.060
Keywords	Allosteric Regulation; Amino Acid Sequence; Base Sequence; Catalytic Domain; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Glucose-1-Phosphate Adenylyltransferase; Kinetics; Molecular Sequence Data; Molecular Weight; Mutation/genetics; Nucleotidyltransferases/chemistry; Nucleotidyltransferases/genetics; Nucleotidyltransferases/isolation & purification; Nucleotidyltransferases/metabolism; Protein Structure, Secondary; Protein Structure, Tertiary; Structure-Activity Relationship; Substrate Specificity
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.