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

Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B.

Chembiochem : a European journal of chemical biology - 1 Jun 2005

Magnusson Anders O, Rotticci-Mulder Johanna C, Santagostino Alberto, Hult Karl

Abstract excerpt

The active site of Candida antarctica lipase B (CALB) hosts the catalytic triad (Ser-His-Asp), an oxyanion hole and a stereospecificity pocket. During catalysis, the fast-reacting enantiomer of secondary alcohols places its medium-sized substituent in the stereospecificity pocket and its large substituent towards the active-site entrance. The largest group to fit comfortably in the stereospecificity pocket is...

Read the complete abstract on PubMed

Topics

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

Share to Alcohols
Share to Candida
Share to Catalysis

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

Share to Fungal Proteins

Share to Lipase

Share to Protein Engineering

Share to Stereoisomerism

Share to Substrate Specificity

Source

Identifiers

PMID: 15883973
DOI: 10.1002/cbic.200400410

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

Creating space for large secondary alcohols by rational redesign of Candida antarctica lipase B.PMID 15883973Read ↗

Laboratory evolution of enantiocomplementary Candida antarctica lipase B mutants with broad substrate scope.Semantic proximity Read ↗

Combinatorial reshaping of the Candida antarctica lipase A substrate pocket for enantioselectivity using an extremely condensed library.Semantic proximity Read ↗

Computational design of a lipase for catalysis of the Diels-Alder reaction.Semantic proximity Read ↗

Activity enhancement of Candida antarctica lipase B by flexibility modulation in helix region surrounding the active site.Semantic proximity Read ↗

Rational creation of mutant enzyme showing remarkable enhancement of catalytic activity and enantioselectivity toward poor substrates.Semantic proximity Read ↗

Mutated variant of Candida antarctica lipase B in (S)-selective dynamic kinetic resolution of secondary alcohols.Semantic proximity Read ↗

Redesign of enzyme for improving catalytic activity and enantioselectivity toward poor substrates: manipulation of the transition state.Semantic proximity Read ↗

Structure, mechanism, and enantioselectivity shifting of lipase LipK107 with a simple way.Semantic proximity Read ↗

Removing the Active-Site Flap in Lipase A from Candida antarctica Produces a Functional Enzyme without Interfacial Activation.Semantic proximity Read ↗

Characterization and Reshaping of a Large and Hydrophobic Nucleophile Pocket in Lipases/Acyltransferases.Semantic proximity Read ↗

Computational approach for designing thermostable Candida antarctica lipase B by molecular dynamics simulation.Semantic proximity Read ↗

Effect of mutations in Candida antarctica B lipase.Semantic proximity Read ↗

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