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.

doi:10.1021/bi00224a008

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Article

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.

Biochemistry - 12 Mar 1991

Labruyère E, Mock M, Surewicz W K, Mantsch H H, Rose T, Munier H, Sarfati R S, Bârzu O

Abstract excerpt

A truncated, 541-residue-long, Bacillus anthracis adenylate cyclase was expressed in Escherichia coli. The purified protein (CYA 62) exhibited catalytic and CaM-binding properties identical with those of the wild-type enzyme secreted by B. anthracis. The analysis of the secondary structure of the CYA 62 protein by Fourier transform infrared spectroscopy and circular dichroism revealed the dominance of beta-type...

Topics

Adenylyl Cyclases
Amino Acid Sequence
Bacillus anthracis
Calmodulin
Catalysis
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Gene Expression Regulation, Bacterial
Gene Expression Regulation, Enzymologic

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Glutamine

Ligands

Lysine

Molecular Sequence Data

Mutation

Spectrometry, Fluorescence

Spectrophotometry, Atomic

Spectrophotometry, Infrared

Temperature

Source

Open in PubMed

Identifiers

PMID: 1900429
DOI: 10.1021/bi00224a008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1900429-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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