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

Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7.

Proteins - 1 Apr 2017

Singh Mrityunjay K, Manoj Narayanan

Abstract excerpt

A conserved cis proline residue located in the active site of Thermotoga maritima acetyl esterase (TmAcE) from the carbohydrate esterase family 7 (CE7) has been substituted by alanine. The residue was known to play a crucial role in determining the catalytic properties of the enzyme. To elucidate the structural role of the residue, the crystal structure of the Pro228Ala variant (TmAcEP228A ) was determined at 2.1...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Biocatalysis
Share to Catalytic Domain

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

Share to Crystallography, X-Ray

Share to Proline

Share to Protein Interaction Domains and Motifs

Share to Protein Structure, Secondary

Share to Thermotoga maritima

Source

Identifiers

PMID: 28097692
DOI: 10.1002/prot.25249

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

Structural role of a conserved active site cis proline in the Thermotoga maritima acetyl esterase from the carbohydrate esterase family 7.PMID 28097692Read ↗

Enhanced catalytic site thermal stability of cold-adapted esterase EstK by a W208Y mutation.Semantic proximity Read ↗

Active site architecture of an acetyl xylan esterase indicates a novel cold adaptation strategy.Semantic proximity Read ↗

Cold-active esterase from Psychrobacter sp. Ant300: gene cloning, characterization, and the effects of Gly-->Pro substitution near the active site on its catalytic activity and stability.Semantic proximity Read ↗

Effect of Cysteine Residue Substitution in the GCSAG Motif of the PMGL2 Esterase Active Site on the Enzyme Properties.Semantic proximity Read ↗

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

Identification of essential arginines in the acetate kinase from Methanosarcina thermophila.Semantic proximity Read ↗

Flexibility and Stability Trade-Off in Active Site of Cold-Adapted Pseudomonas mandelii Esterase EstK.Semantic proximity Read ↗

The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A of Aspergillus fumigatus enhances catalytic activity and thermostability.Semantic proximity Read ↗

On the relevance of the Met-turn methionine in metzincins.Semantic proximity Read ↗

A remote surface loop modulates core structure and cold activity in phosphopantetheine adenylyltransferase.Semantic proximity Read ↗

A bacterial acyl aminoacyl peptidase couples flexibility and stability as a result of cold adaptation.Semantic proximity Read ↗

Carboxyl-peptide plane stacking is important for stabilization of buried E305 of Trichoderma reesei Cel5A.Semantic proximity Read ↗

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