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

Alteration of substrate specificities of thermophilic α/β hydrolases through domain swapping and domain interface optimization.

Acta biochimica et biophysica Sinica - 1 Dec 2012

Zhou Xiaoli, Wang Honglei, Zhang Yuhang, Gao Le, Feng Yan

Abstract excerpt

Protein domain swapping is an efficient way in protein functional evolution in vivo and also has been proved to be an effective strategy to modify the function of the multi-domain proteins in vitro. To explore the potentials of domain swapping for alteration of the enzyme substrate specificities and the structure-function relationship of the homologous proteins, here we constructed two chimeras from a pair of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to Archaeal Proteins

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

Share to Circular Dichroism

Share to Enzyme Stability

Share to Esters

Share to Hydrogen-Ion Concentration

Share to Hydrolases

Share to Nitrophenols

Source

Identifiers

PMID: 23099882
DOI: 10.1093/abbs/gms086

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

Alteration of substrate specificities of thermophilic α/β hydrolases through domain swapping and domain interface optimization.PMID 23099882Read ↗

Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.Semantic proximity Read ↗

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

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

Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily.Semantic proximity Read ↗

Small design from big alignment: engineering proteins with multiple sequence alignment as the starting point.Semantic proximity Read ↗

Modulating Glycoside Hydrolase Activity between Hydrolysis and Transfer Reactions Using an Evolutionary Approach.Semantic proximity Read ↗

Efficiency enhancement in Aspergillus niger α-L-rhamnosidase reverse hydrolysis by using a tunnel site rational design strategy.Semantic proximity Read ↗

Glu88 in the non-catalytic domain of acylpeptide hydrolase plays dual roles: charge neutralization for enzymatic activity and formation of salt bridge for thermodynamic stability.Semantic proximity Read ↗

Engineering the substrate specificity of Alcaligenes D-aminoacylase useful for the production of D-amino acids by optical resolution.Semantic proximity Read ↗

Identification and Mutation Analysis of Nonconserved Residues on the TIM-Barrel Surface of GH5_5 Cellulases for Catalytic Efficiency and Stability Improvement.Semantic proximity Read ↗

Enhancement in catalytic activity of Aspergillus niger XynB by selective site-directed mutagenesis of active site amino acids.Semantic proximity Read ↗

Mutagenesis for Improvement of Activity and Stability of Prolyl Aminopeptidase from Aspergillus oryzae.Semantic proximity Read ↗

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