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

Cofactor specificity switch in Shikimate dehydrogenase by rational design and consensus engineering.

Protein engineering, design & selection : PEDS - 1 Aug 2017

García-Guevara Fernando, Bravo Iris, Martínez-Anaya Claudia, Segovia Lorenzo

Abstract excerpt

Consensus engineering has been used to design more stable variants using the most frequent amino acid at each site of a multiple sequence alignment; sometimes consensus engineering modifies function, but efforts have mainly been focused on studying stability. Here we constructed a consensus Rossmann domain for the Shikimate dehydrogenase enzyme; separately we decided to switch the cofactor specificity through...

Read the complete abstract on PubMed

Topics

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

Share to Alcohol Oxidoreductases
Share to Coenzymes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Consensus Sequence

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Models, Molecular

Share to Protein Engineering

Share to Substrate Specificity

Source

Identifiers

PMID: 28633311
DOI: 10.1093/protein/gzx031

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 · 11 closest

Cofactor specificity switch in Shikimate dehydrogenase by rational design and consensus engineering.PMID 28633311Read ↗

Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations.Semantic proximity Read ↗

Phylogenetic spread of sequence data affects fitness of consensus enzymes: Insights from triosephosphate isomerase.Semantic proximity Read ↗

Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteins.Semantic proximity Read ↗

Shikimate dehydrogenase structure reveals novel fold.Semantic proximity Read ↗

A thermostable phospholipase C obtained by consensus designSemantic proximity Read ↗

Development of a thermostable glucose dehydrogenase by a structure-guided consensus concept.Semantic proximity Read ↗

Thermostabilization of Membrane Proteins by Consensus Mutation: A Case Study for a Fungal Δ8-7 Sterol Isomerase.Semantic proximity Read ↗

The consensus concept for thermostability engineering of proteins.Semantic proximity Read ↗

Divergent evolution of a Rossmann fold and identification of its oldest surviving ancestor.Semantic proximity Read ↗

From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase.Semantic proximity Read ↗

Stabilizing proteins from sequence statistics: the interplay of conservation and correlation in triosephosphate isomerase stability.Semantic proximity Read ↗

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