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Article

Directed molecular evolution of ADP-glucose pyrophosphorylase.

Proceedings of the National Academy of Sciences of the United States of America - 22 Jan 2002

Salamone Peter R, Kavakli I Halil, Slattery Casey J, Okita Thomas W

Abstract excerpt

ADP-glucose pyrophosphorylase catalyzes a rate-limiting reaction in prokaryotic glycogen and plant starch biosynthesis. Despite sharing similar molecular size and catalytic and allosteric regulatory properties, the prokaryotic and higher plant enzymes differ in higher-order protein structure. The bacterial enzyme is encoded by a single gene whose product of ca. 50,000 Da assembles into a homotetrameric structure....

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Identifiers

PMID: 11773627
DOI: 10.1073/pnas.012603799
PMCID: PMC117431

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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