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

Kinetic characterization and ligand binding studies of His351 mutants of Bacillus anthracis adenylate cyclase.

Archives of biochemistry and biophysics - 1 Feb 2006

Gupta Megha, Alam Sheeba, Bhatnagar Rakesh

Abstract excerpt

Edema factor is a calmodulin dependent adenylyl cyclase secreted as one of the primary exotoxins by Bacillus anthracis. A histidine residue at position 351 located in its active site has been implicated in catalysis but direct evidence of its functional role is still lacking. In the present study, we introduced mutations in full-length edema factor (EF) to generate alanine (H351A), asparagine (H351N), and...

Read the complete abstract on PubMed

Topics

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

Share to Adenylyl Cyclases
Share to Alanine
Share to Asparagine

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

Share to Bacillus anthracis

Share to Calmodulin

Share to Catalysis

Share to Histidine

Share to Phenylalanine

Source

Identifiers

PMID: 16386701
DOI: 10.1016/j.abb.2005.11.016

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

Kinetic characterization and ligand binding studies of His351 mutants of Bacillus anthracis adenylate cyclase.PMID 16386701Read ↗

Diminished but Not Abolished Effect of Two His351 Mutants of Anthrax Edema Factor in a Murine Model.Semantic proximity Read ↗

MD simulations of anthrax edema factor: calmodulin complexes with mutations in the edema factor "switch a" region and docking of 3'-deoxy ATP into the adenylyl cyclase active site of wild-type and mutant edema factor variants.Semantic proximity Read ↗

An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis.Semantic proximity Read ↗

Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins.Semantic proximity Read ↗

Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346.Semantic proximity Read ↗

Structure of anthrax edema factor-calmodulin-adenosine 5'-(alpha,beta-methylene)-triphosphate complex reveals an alternative mode of ATP binding to the catalytic site.Semantic proximity Read ↗

Inhibition of the adenylyl cyclase toxin, edema factor, from Bacillus anthracis by a series of 18 mono- and bis-(M)ANT-substituted nucleoside 5'-triphosphates.Semantic proximity Read ↗

Structural basis for the interaction of Bordetella pertussis adenylyl cyclase toxin with calmodulin.Semantic proximity Read ↗

A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis.Semantic proximity Read ↗

The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme.Semantic proximity Read ↗

Structure-function relationships in Escherichia coli adenylate cyclase.Semantic proximity Read ↗

Soluble expression and purification of the anthrax protective antigen in E. coli and identification of a novel dominant-negative mutant N435C.Semantic proximity Read ↗

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