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

Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C.

The Journal of biological chemistry - 4 Jul 2003

Feng Jianwen, Bradley William D, Roberts Mary F

Abstract excerpt

The phosphatidylinositol-specific phospholipase C from Bacillus thuringiensis can be activated by nonsubstrate interfaces such as phosphatidylcholine micelles or bilayers. This activation corresponds with partial insertion into the interface of two tryptophans, Trp-47 in helix B and Trp-242 in a loop, in the rim of the alphabeta-barrel. Both W47A and W242A have much weaker binding to interfaces and considerably...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus thuringiensis
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Dyes

Share to Phosphatidylinositol Diacylglycerol-Lyase

Share to Phosphoinositide Phospholipase C

Share to Phosphotransferases

Share to Tryptophan

Share to Type C Phospholipases

Source

Identifiers

PMID: 12714598
DOI: 10.1074/jbc.M301207200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C.PMID 12714598Read ↗

Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C.Semantic proximity Read ↗

Role of helix B residues in interfacial activation of a bacterial phosphatidylinositol-specific phospholipase C.Semantic proximity Read ↗

Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C.Semantic proximity Read ↗

Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface.Semantic proximity Read ↗

Cation-π interactions as lipid-specific anchors for phosphatidylinositol-specific phospholipase C.Semantic proximity Read ↗

Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C.Semantic proximity Read ↗

Structure of the S. aureus PI-specific phospholipase C reveals modulation of active site access by a titratable π-cation latched loop.Semantic proximity Read ↗

The catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad in phosphatidylinositol-specific phospholipase C can be substituted by a chloride ion.Semantic proximity Read ↗

Construction of Aspergillus niger lipase mutants with oil-water interface independence.Semantic proximity Read ↗

Altering the activation mechanism in Thermomyces lanuginosus lipase.Semantic proximity Read ↗

Role of the Tryptophan Residues in the Specific Interaction of the Sea Anemone Stichodactyla helianthus's Actinoporin Sticholysin II with Biological Membranes.Semantic proximity Read ↗

Engineering of Bacillus lipase by directed evolution for enhanced thermal stability: effect of isoleucine to threonine mutation at protein surface.Semantic proximity Read ↗

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