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

Conformational stability of esterase enzymes from different sources.

Protein and peptide letters - 1 Jan 2009

Del Vecchio Pompea, Graziano Giuseppe, Barone Guido

Abstract excerpt

In the last years we have performed a series of studies to characterize the conformational stability of three esterases from thermophilic and mesophilic sources: Aes esterase from Escherichia coli, EST2 from Alicyclobacillus acidocaldarius and AFEST from Archeoglobus fulgidus. These three esteras...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to Carboxylic Ester Hydrolases
Share to Circular Dichroism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Enzyme Stability

Share to Esterases

Share to Guanidine

Share to Sterol Esterase

Source

Identifiers

PMID: 19508182
DOI: 10.2174/092986609789071315

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19508182-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conformational stability of esterase enzymes from different sources.PMID 19508182Read ↗

Role of the N-terminal region for the conformational stability of esterase 2 from Alicyclobacillus acidocaldarius.Semantic proximity Read ↗

Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.Semantic proximity Read ↗

Analysis of thermal adaptation in the HSL enzyme family.Semantic proximity Read ↗

The crystal structure of an EST2 mutant unveils structural insights on the H group of the carboxylesterase/lipase family.Semantic proximity Read ↗

Comprehensive analysis of surface charged residues involved in thermal stability in Alicyclobacillus acidocaldarius esterase 2.Semantic proximity Read ↗

Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties.Semantic proximity Read ↗

Functional and structural features of the oxyanion hole in a thermophilic esterase from Alicyclobacillus acidocaldarius.Semantic proximity Read ↗

A substrate-induced switch in the reaction mechanism of a thermophilic esterase: kinetic evidences and structural basis.Semantic proximity Read ↗

Role of key salt bridges in thermostability of G. thermodenitrificans EstGtA2: distinctive patterns within the new bacterial lipolytic enzyme subfamily XIII.2 [corrected].Semantic proximity Read ↗

Stability curves of laboratory evolved thermostable mutants of a Bacillus subtilis lipase.Semantic proximity Read ↗

Mapping the Accessible Conformational Landscape of an Insect Carboxylesterase Using Conformational Ensemble Analysis and Kinetic CrystallographySemantic proximity Read ↗

In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation.Semantic proximity Read ↗

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