Discover Community Create You

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

Article

Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution.

Proceedings of the National Academy of Sciences of the United States of America - 18 Mar 2003

Williams Gavin J, Domann Silvie, Nelson Adam, Berry Alan

Abstract excerpt

Aldolases have potential as tools for the synthesis of stereochemically complex carbohydrates. Here, we show that directed evolution can be used to alter the stereochemical course of the reaction catalyzed by tagatose-1,6-bisphosphate aldolase. After three rounds of DNA shuffling and screening, the evolved aldolase showed an 80-fold improvement in k(cat)/K(m) toward the non-natural substrate fructose...

Read the complete abstract on PubMed

Topics

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

Share to Aldehyde-Lyases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Directed Molecular Evolution

Share to Kinetics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Recombinant Proteins

Share to Stereoisomerism

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 12626743
DOI: 10.1073/pnas.0635924100
PMCID: PMC152260

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modifying the stereochemistry of an enzyme-catalyzed reaction by directed evolution.PMID 12626743Read ↗

Enhancing one-step d-tagatose production from d-fructose through combinatorial structure-guided and evolution-based engineering of tagatose 4-epimerase.Semantic proximity Read ↗

Creation of the first anomeric D/L-sugar kinase by means of directed evolution.Semantic proximity Read ↗

Structure-based engineering of E. coli galactokinase as a first step toward in vivo glycorandomization.Semantic proximity Read ↗

Directed evolution of a new catalytic site in 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli.Semantic proximity Read ↗

Harnessing l-arabinose isomerase for biological production of d-tagatose: Recent advances and its applicationsSemantic proximity Read ↗

Directed evolution of D-sialic acid aldolase to L-3-deoxy-manno-2-octulosonic acid (L-KDO) aldolase.Semantic proximity Read ↗

Structure-Guided Directed Evolution of Glycosidases: A Case Study in Engineering a Blood Group Antigen-Cleaving Enzyme.Semantic proximity Read ↗

Manipulating the expression rate and enantioselectivity of an epoxide hydrolase by using directed evolution.Semantic proximity Read ↗

Mutability-Landscape-Guided Engineering of l-Threonine Aldolase Revealing the Prelog Rule in Mediating Diastereoselectivity of C-C Bond Formation.Semantic proximity Read ↗

Structure-based enhancement of the first anomeric glucokinase.Semantic proximity Read ↗

Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage.Semantic proximity Read ↗

Improving upon nature: active site remodeling produces highly efficient aldolase activity toward hydrophobic electrophilic substrates.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.