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Article

Structural elements in IGP synthase exclude water to optimize ammonia transfer.

Biophysical journal - 1 Jul 2005

Amaro Rommie E, Myers Rebecca S, Davisson V Jo, Luthey-Schulten Zaida A

Abstract excerpt

In the complex pathway of histidine biosynthesis, a key branch point linking amino acid and purine biosynthesis is catalyzed by the bifunctional enzyme imidazole glycerol phosphate (IGP) synthase. The first domain of IGP synthase, a triad glutamine amidotransferase, hydrolyzes glutamine to form glutamate and ammonia. Its activity is tightly regulated by the binding of the substrate PRFAR to its partner synthase...

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Identifiers

PMID: 15849257
DOI: 10.1529/biophysj.104.058651
PMCID: PMC1366548

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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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