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1986•FEMS Microbiology LettersRequires access

A new peptidoglycan hydrolase in Streptococcus pneumoniae

José-María Sánchez-Puelles

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Abstract

The use of a mutant of Streptococcus pneumoniae deleted in the lytA gene coding for the N-acetyl-muramyl-l-alanine amidase, and therefore devoid of any amidase, has allowed the identification of a new murein hydrolase activity in this bacterium. This enzyme (or enzymes) acted as an autolysin when the cultures were grown at 30°C. Our results strongly suggest that the new lytic activity corresponds to one or more glycosidases.

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What this paper is about

The use of a mutant of Streptococcus pneumoniae deleted in the lytA gene coding for the N-acetyl-muramyl-l-alanine amidase, and therefore devoid of any amidase, has allowed the identification of a new murein hydrolase activity in this bacterium. This enzyme (or enzymes) acted as an autolysin when the cultures were grown at 30°C. Our results strongly suggest that the new lytic activity corresponds to one or more glycosidases.

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Available abstract

The use of a mutant of Streptococcus pneumoniae deleted in the lytA gene coding for the N-acetyl-muramyl-l-alanine amidase, and therefore devoid of any amidase, has allowed the identification of a new murein hydrolase activity in this bacterium. This enzyme (or enzymes) acted as an autolysin when the cultures were grown at 30°C. Our results strongly suggest that the new lytic activity corresponds to one or more glycosidases.

Key concepts: Autolysin, Amidase, Peptidoglycan, Streptococcus pneumoniae, Lytic cycle, Hydrolase, Microbiology, Muramidase

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