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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

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

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Source

Identifiers

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

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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

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

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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 ↗

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