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

Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.

Protein engineering, design & selection : PEDS - 1 May 2008

Koutsioulis Dimitris, Wang Ellen, Tzanodaskalaki Maria, Nikiforaki Dimitra, Deli Alexandra, Feller Georges, Heikinheimo Pirkko, Bouriotis Vassilis

Abstract excerpt

Psychrophilic alkaline phosphatase (AP) from the Antarctic strain TAB5 was subjected to directed evolution in order to identify the key residues steering the enzyme's cold-adapted activity and stability. A round of random mutagenesis and further recombination yielded three thermostable and six thermolabile variants of the TAB5 AP. All of the isolated variants were characterised by their residual activity after...

Read the complete abstract on PubMed

Topics

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

Share to Alkaline Phosphatase
Share to Calorimetry, Differential Scanning

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to Directed Molecular Evolution

Share to Protein Denaturation

Share to Protein Engineering

Share to Protein Folding

Share to Thermodynamics

Source

Identifiers

PMID: 18411226
DOI: 10.1093/protein/gzn009

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

Directed evolution on the cold adapted properties of TAB5 alkaline phosphatase.PMID 18411226Read ↗

Crystal structure of alkaline phosphatase from the Antarctic bacterium TAB5.Semantic proximity Read ↗

Engineered disulfide bonds increase active-site local stability and reduce catalytic activity of a cold-adapted alkaline phosphatase.Semantic proximity Read ↗

Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases.Semantic proximity Read ↗

Structural and functional characterization of a cold-adapted stand-alone TPM domain reveals a relationship between dynamics and phosphatase activity.Semantic proximity Read ↗

Artificial evolution of an enzyme active site: structural studies of three highly active mutants of Escherichia coli alkaline phosphatase.Semantic proximity Read ↗

Cold adaptation of a psychrophilic chitinase: a mutagenesis study.Semantic proximity Read ↗

Consistent mutational paths predict eukaryotic thermostability.Semantic proximity Read ↗

Comprehensive mutagenesis to identify amino acid residues contributing to the difference in thermostability between two originally thermostable ancestral proteins.Semantic proximity Read ↗

Turning a mesophilic protein into a thermophilic one: a computational approach based on 3D structural features.Semantic proximity Read ↗

Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight.Semantic proximity Read ↗

Stepwise adaptations to low temperature as revealed by multiple mutants of psychrophilic α-amylase from Antarctic Bacterium.Semantic proximity Read ↗

Contribution of engineered electrostatic interactions to the stability of cytosolic malate dehydrogenase.Semantic proximity Read ↗

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