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Article

The ADP-glucose pyrophosphorylase from Escherichia coli comprises two tightly bound distinct domains.

FEBS letters - 27 Aug 2004

Bejar Clarisa M, Ballicora Miguel A, Gómez-Casati Diego F, Iglesias Alberto A, Preiss Jack

Abstract excerpt

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...

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Identifiers

PMID: 15327982
DOI: 10.1016/j.febslet.2004.07.060

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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