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Teichoicase from Bacillus subtilis Marburg.

W Kusser, F Fiedler

Journal of Bacteriology

|July 1, 1983

Summary

This summary is machine-generated.

Researchers describe a teichoicase enzyme from Bacillus subtilis Marburg that degrades specific cell wall components. This enzyme offers potential for detecting and modifying bacterial surfaces.

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Area of Science:

Microbiology
Enzymology
Biochemistry

Background:

Teichoic acids are essential cell wall components in Gram-positive bacteria, particularly Bacillus subtilis.
Understanding enzymes that modify teichoic acids is crucial for bacterial cell wall research.

Purpose of the Study:

To characterize a novel teichoic acid-degrading enzyme (teichoicase) from Bacillus subtilis Marburg.
To investigate the enzyme's substrate specificity, mechanism of action, and regulation.

Main Methods:

Purification and characterization of the teichoicase enzyme.
Assays for phosphodiesterase and phosphomonoesterase activity.
Analysis of enzyme activity in Bacillus subtilis mutants and culture supernatants.

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Main Results:

The purified teichoicase exhibits phosphodiesterase activity specific for alpha-glucosylated glycerol teichoic acid.
Degradation occurs via an exo-mechanism, releasing a specific monomer.
Enzyme activity is linked to sporulation, present in stage II mutants but absent in stage O mutants.
The enzyme is active on producing cells, with products detected in the supernatant.

Conclusions:

Teichoicase from Bacillus subtilis Marburg is a specific phosphodiesterase targeting endogenous cell wall teichoic acid.
Its activity is associated with bacterial sporulation.
The enzyme has potential applications in detecting specific teichoic acids and modifying bacterial surfaces.