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 changes leading to increased enzymatic activity in an engineered variant of Bacillus lentus subtilisin.

Advances in experimental medicine and biology - 1 Jan 1996

Bott R, Dauberman J, Wilson L, Ganshaw G, Sagar H, Graycar T, Estell D

Abstract excerpt

No abstract is available from the source.

Topics

Bacillus
Computer Graphics
Genetic Variation
Hydrogen Bonding
Hydrolysis
Kinetics
Mutagenesis, Site-Directed
Protein Engineering
Serine
Structure-Activity Relationship
Subtilisins

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 8796332
DOI: 10.1007/978-1-4613-0319-0_29

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural changes leading to increased enzymatic activity in an engineered variant of Bacillus lentus subtilisin.PMID 8796332Read ↗

Studies on the structure and function of subtilisin E by protein engineering.Semantic proximity Read ↗

Protein engineering of subtilisin.Semantic proximity Read ↗

Synergistic Mutations Create Bacillus Subtilisin Variants with Enhanced Poly-l-Lactic Acid Depolymerization Activity.Semantic proximity Read ↗

Structure and function of subtilisin BPN' as studied through crystallographic studies on a series of its complexes with genetically engineered proteinaceous inhibitor SSI.Semantic proximity Read ↗

Covalent modification of subtilisin Bacillus lentus cysteine mutants with enantiomerically pure chiral auxiliaries causes remarkable changes in activity.Semantic proximity Read ↗

A multifunctional α-amylase BSGH13 from Bacillus subtilis BS-5 possessing endoglucanase and xylanase activities.Semantic proximity Read ↗

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

Crystal structure analysis of subtilisin BPN' mutants engineered for studying thermal stability.Semantic proximity Read ↗

Enhancing thermostabilization of a newly discovered α-amylase from Bacillus cereus GL96 by combining computer-aided directed evolution and site-directed mutagenesis.Semantic proximity Read ↗

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

Engineering surface loops of proteins--a preferred strategy for obtaining new enzyme function.Semantic proximity Read ↗

Active site binding loop stabilization in the subtilisin inhibitor eglin c: structural and functional studies on specifically designed mutants in complex with subtilisin and the uncomplexed inhibitor.Semantic proximity Read ↗

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