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Article

Directed Evolution Mimics Allosteric Activation by Stepwise Tuning of the Conformational Ensemble.

Journal of the American Chemical Society - 13 Jun 2018

Buller Andrew R, van Roye Paul, Cahn Jackson K B, Scheele Remkes A, Herger Michael, Arnold Frances H

Abstract excerpt

Allosteric enzymes contain a wealth of catalytic diversity that remains distinctly underutilized for biocatalysis. Tryptophan synthase is a model allosteric system and a valuable enzyme for the synthesis of noncanonical amino acids (ncAA). Previously, we evolved the β-subunit from Pyrococcus furiosus, PfTrpB, for ncAA synthase activity in the absence of its native partner protein PfTrpA. However, the precise...

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Identifiers

PMID: 29712420
DOI: 10.1021/jacs.8b03490
PMCID: PMC5999571

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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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