the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
the two major cell wall recycling enzymes are AmgK and MurU. This specific cell wall recycling machinery, present in many bacterial species including Pseudomonas putida, includes the recycling enzyme AmgK that converts NAM into MurNAc 1-phosphate, which is then converted to UDP-MurNAc (UDP-NAM) by MurU. These enzymes produce UDP-NAM, a critical precursor involved in the initial steps of the bacterial cell wall biosynthesis. Peptidoglycan biosynthetic and recycling pathway, overview
enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity
the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
the metabolic pathway of anomeric cell wall amino sugar kinase AmgK and uridylyl transferase MurU converts N-acetylmuramic acid to uridine diphosphate-N-acetylmuramic acid. It is responsible for the high intrinsic resistance of Pseudomonas aeruginosa to fosfomycin due to bypassing the fosfomycin-sensitive de novo synthesis of UDP-N-acetylmuramic acid
enzyme is involved in a salvage pathway in Gram-negative bacteria that bypasses de novo biosynthesis of UDP N-acetylmuramic acid. The pathway consisits of anomeric sugar kinase AmgK and the MurNAc alpha-1-phosphate uridylyl transferase MurU. Deletion of the encoding gene increases fosfomycin sensitivity
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
the bacterial cell wall recycling enzymes MurNAc/GlcNAc anomeric kinase (AmgK) and NAM alpha-1 phosphate uridylyl transferase (MurU) are permissive to permutations at the two and three positions of the sugar donor. Utility of these derivatives in the fluorescent labeling of both Gram(-) and Gram(+) peptidoglycan in whole cells using a variety of bioorthogonal chemistries including the tetrazine ligation, allowing a rapid and scalable access to a variety of functionalized NAMs and UDP NAMs, for synthetic and purification strategies to access large quantities of these PG building blocks, and derivatives, overview
utility of bacterial peptidoglycan recycling enzymes, AmgK and MurU, in the chemoenzymatic synthesis of valuable UDP-sugar substrates. AmgK and MurU are used in situ to produce UDP-NAMs substrates which are subsequently used in in vivo labeling experiments. Synthesis of several 2-amino and N-acetyl muramic acid derivatives, method, detailed overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged MurU from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, tag cleavage by PreScission protease, and gel filtration
Renner-Schneck, M.; Hinderberger, I.; Gisin, J.; Exner, T.; Mayer, C.; Stehle, T.
Crystal structure of the N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, a minimal sugar nucleotidyltransferase and potential drug target enzyme in Gram-negative pathogens