Identification and in vitro Analysis of the GatD/MurT Enzyme-Complex Catalyzing Lipid II Amidation in Staphylococcus aureus

• Published in: PLoS pathogens Vol. 8; no. 1; p. e1002509
• Main Authors: Münch, Daniela, Roemer, Terry, Lee, Sang Ho, Engeser, Marianne, Sahl, Hans Georg, Schneider, Tanja
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 01.01.2012; Public Library of Science (PLoS)
• Subjects: Animals; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Bacterial Proteins - metabolism; Bacteriology; Biology; Catalysis; Cell Wall - enzymology; Cell Wall - genetics; Crosslinked polymers; Enzymes; Humans; Immunity, Innate - physiology; Inactivation; Lipids; Medicine; Microbiological chemistry; Microbiology; Multienzyme Complexes - genetics; Multienzyme Complexes - immunology; Multienzyme Complexes - metabolism; Mutation; Operon - physiology; Peptides; Peptidoglycans; Physiological aspects; Proteins; Signal Transduction - physiology; Staphylococcal Infections - enzymology; Staphylococcal Infections - genetics; Staphylococcal Infections - immunology; Staphylococcus aureus; Staphylococcus aureus - enzymology; Staphylococcus aureus - genetics; Staphylococcus aureus - immunology; Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives; Uridine Diphosphate N-Acetylmuramic Acid - genetics; Uridine Diphosphate N-Acetylmuramic Acid - immunology; Uridine Diphosphate N-Acetylmuramic Acid - metabolism; Germany

The peptidoglycan of Staphylococcus aureus is characterized by a high degree of crosslinking and almost completely lacks free carboxyl groups, due to amidation of the D-glutamic acid in the stem peptide. Amidation of peptidoglycan has been proposed to play a decisive role in polymerization of cell w...