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Article

Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization.

Biochimica et biophysica acta - 1 Dec 2011

Pearce F Grant, Dobson Renwick C J, Jameson Geoffrey B, Perugini Matthew A, Gerrard Juliet A

Abstract excerpt

To gain insights into the role of quaternary structure in the TIM-barrel family of enzymes, we introduced mutations to the DHDPS enzyme of Thermotoga maritima, which we have previously shown to be a stable tetramer in solution. These mutations were aimed at reducing the number of salt bridges at one of the two tetramerization interface of the enzyme, which contains many more interactions than the well...

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Identifiers

PMID: 21803176
DOI: 10.1016/j.bbapap.2011.07.016

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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