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

In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates.

Journal of molecular biology - 12 Jan 2001

Matsumura I, Ellington A D

Abstract excerpt

The Escherichia coli beta-glucuronidase (GUS) was evolved in vitro to catalyze the hydrolysis of a beta-galactoside substrate 500 times more efficiently (k(cat)/K(m)) than the wild-type, with a 52 million-fold inversion in specificity. The amino acid substitutions that recurred among 32 clones isolated in three rounds of DNA shuffling and screening were mapped to the active site. The functional consequences of...

Read the complete abstract on PubMed

Topics

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

Share to beta-Galactosidase
Share to Directed Molecular Evolution
Share to Galactosides

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

Share to Glucuronic Acid

Share to Glucuronidase

Share to Protein Conformation

Share to Protein Engineering

Share to Substrate Specificity

Source

Identifiers

PMID: 11124909
DOI: 10.1006/jmbi.2000.4259

Provenance

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates.PMID 11124909Read ↗

Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop.Semantic proximity Read ↗

A comparison of directed evolution approaches using the beta-glucuronidase model system.Semantic proximity Read ↗

Conversion of a cyclodextrin glucanotransferase into an alpha-amylase: assessment of directed evolution strategies.Semantic proximity Read ↗

Increasing the thermal stability of an oligomeric protein, beta-glucuronidase.Semantic proximity Read ↗

Determining the evolutionary potential of a gene.Semantic proximity Read ↗

Bottom-up single-molecule strategy for understanding subunit function of tetrameric β-galactosidase.Semantic proximity Read ↗

[Molecular evolution of beta-glucuronidase in vitro: obtaining thermotolerant GUS gene].Semantic proximity Read ↗

The mutability of enzyme active-site shape determinants.Semantic proximity Read ↗

Random exchanges of non-conserved amino acid residues among four parental termite cellulases by family shuffling improved thermostability.Semantic proximity Read ↗

Directed evolution of a beta-galactosidase from Pyrococcus woesei resulting in increased thermostable beta-glucuronidase activity.Semantic proximity Read ↗

Enzyme activity engineering based on sequence co-evolution analysis.Semantic proximity Read ↗

Catalytic consequences of experimental evolution: catalysis by a 'third-generation' evolvant of the second beta-galactosidase of Escherichia coli, ebgabcde, and by ebgabcd, a 'second-generation' evolvant containing two supposedly 'kinetically silent' mutations.Semantic proximity Read ↗

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