Distal Mutations in a Designed Retro-Aldolase Alter Loop Dynamics to Shift and Accelerate the Rate-Limiting Step.

doi:10.1021/jacs.5c05134

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

Distal Mutations in a Designed Retro-Aldolase Alter Loop Dynamics to Shift and Accelerate the Rate-Limiting Step.

Journal of the American Chemical Society - 27 Aug 2025

Hunt Serena E, Klaus Cindy, John Aqza E, Zarifi Niayesh, Martinez Alec, Feixas Ferran, Garcia-Borràs Marc, Thompson Michael C, Chica Roberto A

Abstract excerpt

Amino acid residues distant from an enzyme's active site are known to influence catalysis, but their mechanistic contributions to the catalytic cycle remain poorly understood. Here, we investigate the structural, functional, and mechanistic impacts of distal and active-site mutations discovered through directed evolution of the computationally designed retro-aldolase RA95. Active-site mutations improve catalytic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Biocatalysis
Share to Catalytic Domain
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Fructose-Bisphosphate Aldolase

Share to Kinetics

Share to Molecular Dynamics Simulation

Share to Mutation

Source

Open in PubMed

Identifiers

PMID: 40802856
DOI: 10.1021/jacs.5c05134

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.