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J Bacteriol. 1971 September; 107(3): 697-703
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Structure of the Cell Wall of Bacillus stearothermophilus: Mode of Action of a Thermophilic Bacteriophage Lytic Enzyme

¹ Department of Biological Sciences, Northwestern University, Evanston, Illinois 60201

ABSTRACT

The mode of action of a bacteriophage lytic enzyme on cell walls of Bacillus stearothermophilus (NCA 1503-4R) has been investigated. The enzyme is an endopeptidase which catalyzes the hydrolysis of the L-alanyl-D-glutamyl linkage in peptide subunits of the cell wall peptidoglycan. Preliminary studies on the soluble components in lytic cell wall digests indicate that the glycan moiety is composed of alternating glucosamine and muramic acid; one half of the muramic acid residues contain the tripeptide, L-alanyl-D-glutamyldiaminopimelic acid, and the remaining residues contain the tetrapeptide, L-alanyl-D-glutamyldiaminopimeyl-D-alanine. Almost one half of the peptide subunits are involved in cross-linkages of chemotype I. A structure for the cell wall peptidoglycan is proposed in the light of these findings.