Identification and in vitro Analysis of the GatD/MurT Enzyme-Complex Catalyzing Lipid II Amidation in Staphylococcus aureus
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...
Main Authors: | Münch, Daniela, Roemer, Terry, Lee, Sang Ho, Engeser, Marianne, Sahl, Hans Georg, Schneider, Tanja |
---|---|
Format: | Online |
Language: | English |
Published: |
Public Library of Science
2012
|
Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3266927/ |
Similar Items
-
Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus
by: Erik R. Nöldeke, et al.
Published: (2018-08-01) -
Specificity Determinants for Lysine Incorporation in Staphylococcus aureus Peptidoglycan as Revealed by the Structure of a MurE Enzyme Ternary Complex*
by: Ruane, Karen M., et al.
Published: (2013) -
Conversion of Amides to Esters by the Nickel-Catalyzed Activation of Amide C–N Bonds
by: Hie, Liana, et al.
Published: (2015) -
The Staphylococcus aureus Membrane Protein SA2056 Interacts with Peptidoglycan Synthesis Enzymes
by: Quiblier, Chantal, et al.
Published: (2013) -
Copper-Catalyzed
Intermolecular Amidation and Imidation
of Unactivated Alkanes
by: Tran, Ba L., et al.
Published: (2014)