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

Substrate specificity of natural variants and genetically engineered intermediates of Bacillus lentus alkaline proteases.

Advances in experimental medicine and biology - 1 Jan 1996

Maurer K H, Markgraf M, Goddette D

Abstract excerpt

Three natural variants of subtilisin lentus could be differentiated by their amino acid sequence and their specific activity with low molecular weight peptide substrates of the type sAAPFpNA. The variants had amino acid exchanges in five, respective six positions of their amino acid sequence, four of which are located in the substrate loop of the enzyme (positions 92 - 102). Variants of one type of highly...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Base Sequence
Share to Genetic Variation

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

Share to Hydrogen-Ion Concentration

Share to Models, Molecular

Share to Molecular Sequence Data

Share to Mutagenesis, Site-Directed

Share to Substrate Specificity

Source

Identifiers

PMID: 8796329
DOI: 10.1007/978-1-4613-0319-0_26

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

Substrate specificity of natural variants and genetically engineered intermediates of Bacillus lentus alkaline proteases.PMID 8796329Read ↗

Probing the altered specificity and catalytic properties of mutant subtilisin chemically modified at position S156C and S166C in the S1 pocket.Semantic proximity Read ↗

Variants of subtilisin BPN' with altered specificity profiles.Semantic proximity Read ↗

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

Substrate specificity of trypsin investigated by using a genetic selection.Semantic proximity Read ↗

Unusual ligand binding at the active site domain of an engineered mutant of subtilisin BL.Semantic proximity Read ↗

Selection of Streptomyces griseus protease B mutants with desired alterations in primary specificity using a library screening strategy.Semantic proximity Read ↗

Engineering substrate preference in subtilisin: structural and kinetic analysis of a specificity mutant.Semantic proximity Read ↗

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

Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'.Semantic proximity Read ↗

The effect of changing the hydrophobic S1' subsite of thermolysin-like proteases on substrate specificity.Semantic proximity Read ↗

Structural basis for broad specificity in alpha-lytic protease mutants.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 ↗

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