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Article

A study of Escherichia coli adenylosuccinate synthetase association states and the interface residues of the homodimer.

The Journal of biological chemistry - 14 Mar 1997

Wang W, Gorrell A, Honzatko R B, Fromm H J

Abstract excerpt

The state of aggregation of adenylosuccinate synthetase from Escherichia coli is a point of controversy, with crystal structures indicating a dimer and some solution studies indicating a monomer. Crystal structures implicate Arg143 and Asp231 in stabilizing the dimer, with Arg143 interacting directly with bound IMP of the 2-fold related subunit. Residue Arg143 was changed to Lys and Leu, and residue Asp231 was...

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PMID: 9054400
DOI: 10.1074/jbc.272.11.7078

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

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