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malfunction
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inhibition of the enzyme blocks peptidoglycan synthesis and leads to bacterial lysis and death
metabolism
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the enzyme also functions as an activity enhancer of SpoIIP which generates its substrate
additional information
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the enzyme contain a conserved hydrophobic surface that mediates its interaction with the cytoplasmic membrane and renders the purified protein polydisperse. Quantitative binding study of the MtgA by surface plasmon resonance
evolution

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the enzyme belongs to the glycosyltransferases of family 51 (GT51), the glycosyltransferases of family 51 are essential enzymes found in bacteria with peptidoglycan cell wall. They exist in two forms: as a monofunctional domain or linked to the N-terminal end of penicillin-binding (PB) domain in bifunctional PB proteins. Both forms catalyze the polymerization of lipid II (undecaprenyl pyrophosphate-MurNAc(pentapeptide)-GlcNAc) precursor to form linear glycan chains
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs; proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs; proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs; proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Escherichia coli has 3 class A PBPs (PBP1a, PBP1b, and PBP1c) and 2 MGT proteins
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evolution
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proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs; proteins with PGT activity occur as monofunctional glycosyltransferases (MGTs) and as bifunctional penicillin-binding proteins (PBPs) designated as class A PBPs. Both forms contain a single transmembrane span at the N-terminus followed by the glycosyltransferase domain. In the class A PBPs, the C-terminus contains the transpeptidase domain. Bacterial species typically have multiple forms of these enzymes. Staphylococcus aureus has a single class A PBP (PBP2) and 2 MGT proteins (SgtA, SgtB/MGT)
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physiological function

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isoform PBP3 is required for localization of MurG to division site
physiological function
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PGT catalyzes the polymerization of lipid II to form the bacterial cell wall
physiological function
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MtgA localizes at the division site of Escherichia coli cells that are deficient in PBP1b and produce a thermosensitive PBP1a and is able to interact with three constituents of the divisome, PBP3, FtsW, and FtsN in peptidoglycan assembly during the cell cycle
physiological function
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pbp-1C gene regulates in vitro growth and cell morphology, whereas pbp-1A, pbp-1B, and pbp-2 genes are essential for viability of Brucella melitensis
physiological function
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the enzyme catalyze the polymerization of lipid II to form linear glycan chains, which, after cross linking by the transpeptidases, form the net-like peptidoglycan macromolecule, which encases bacteria and protects them from rupture under their high cytoplasmic pressure
physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP); the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP); the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
physiological function
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the enzyme is involved in synthesis of peptidoglycan, a key cell wall component in nearly all bacteria, protecting the cell from bursting by its internal turgor and maintaining cell shape. Peptidoglycan consists of glycan strands connected by short peptides and forms a continuous, mesh-like structure around the cytoplasmic membrane, called the sacculus. In Gram-negative species, such as Escherichia coli, the sacculus is made of a mainly single layer of peptidoglycan with a thickness of 3-6 nm. The glycan strands are made of alternating N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc) residues linked by beta-1,4 glyosidic bonds. The peptides contain L- and D-amino acids and are linked to MurNAc residues. The sequence is L-Ala-D-iGlu-m-Dap-D-Ala-D-Ala (m-Dap, meso-diaminopimelic acid). During cell growth and division, the surface of the sacculus is enlarged by the incorporation of new peptidoglycan material. In this process, the precursor lipid II (undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc) is polymerized by the glycosyltransferase reaction of the GTase domain of enzyme PBP1B
physiological function
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synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP); the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
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physiological function
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bifunctional penicillin-binding proteins (PBPs) proceed and catalyze the transglycosylation and transpeptidation. Bifunctional PBPs have both glycosyltransferase and transpeptidase catalytic sites that are located at N-terminus and C-terminus, respectively. In transglycosylation step, the glycosyltransferase polymerizes disaccharide phospholipid lipid II into polysaccharide strands. These oligosaccharide strands are cross-linked by transpeptidase to form peptidoglycans in the next transpeptidation step; synthesis of bacterial cell wall requires the concerted action of peptidoglycan glycosyltransferases (PGT, also known as peptidoglycan transglycosylases) and transpeptidases. The PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing TP enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate (C55PP); the PGT enzymes transfer the disaccharide-peptide from the lipid II substrate onto the growing glycan chain allowing transpeptidase enzymes to crosslink peptides from adjacent chains. The lipid II substrate is anchored into the cell membrane through an undecaprenyl (C55) tail. The enzymatic reaction is thought to occur at the surface of the membrane
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undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc + undecaprenyl-diphosphoryl-MurNAc-(L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala)-GlcNAc
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
[phenyl-4(n)-3H]benzylpenicillin
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additional information
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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enzyme synthesizes lysozyme-sensitive peptidoglycan from undecaprenyldiphosphoryl-disaccharide-pentapeptide
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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enzyme synthesizes lysozyme-sensitive peptidoglycan from undecaprenyldiphosphoryl-disaccharide-pentapeptide
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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for isoform PBP2A, the limiting length of produced glycan chains is about 15 disaccharide units
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
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for isoform PBP1B, the limiting length of produced glycan chains is about 50 disaccharide units, whereas it is about 30 disaccharide units for isoform PBP1A
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?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
peptidoglycan-synthetic enzyme activities of penicillin-binding protein 3 may by involved in the process of cell division
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
enzyme is involved in synthesis of peptidoglycan
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
PBP1a and PBP1b have both transglycosylase and transpeptidase activity
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
the enzyme catalyzes the assembly of lipid-transported N-acetylglucosaminyl-beta-1,4-N-acetylmuramoyl-L-Ala-gamma-D-Glu-meso-(diaminopimelic acid)-D-Ala-D-Ala units (lipid II) into linear peptidoglycan chains. These units are linked, at C1 of N-acetylmuramic acid, to a C55 undecaprenyl diphosphate. In an in vitro assay, lipid II functions both as a glycosyl donor and as a glycosyl acceptor substrate. Using substrate analogues, it is suggested that the specificity of the enzyme for the glycosyl donor substrate differs from that for the acceptor. The donor substrate requires the presence of both N-acetylglucosamine and MurNAc and a reactive group on C1 of the MurNAc and does not absolutely require the lipid chain which can be replaced by uridine. The enzyme appears to prefer an acceptor substrate containing a polyprenyl pyrophosphate on C1 of the MurNAc sugar
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
glycosyltransferase activity catalyzes glycan chain elongation from lipid II substrate undecaprenyl-pyrophosphoryl-N-acetylglucosamine-N-acetylmuramic acid-pentapeptide. PBP4 also catalyzes the aminolysis (D-Ala as acceptor) and hydrolysis of the thiolester donor substrate benzoyl-Gly-thioglycolate, indicating that PBP4 possesses both transpeptidase and carboxypeptidase activities
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
for isoform PBP2, the limiting length of produced glycan chains is about 15 disaccharide units
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
additional information

?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
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-
the enzyme is both an amidase and an endopeptidase. The enzyme is a lytic transglycosylase that degrades the glycan strands of the peptidoglycan into disaccharide units. The enzyme binds the cell wall, but only cleaves the glycan strands after the stem peptides have been removed. The enzyme alone is unable to cleave purified peptidoglycan but needs the presence of SpoIIP
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-
-
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
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-
the enzyme shows both transglycosylase and transpeptidase activities
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-
-
additional information
?
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-
overproduction of the inactive PBP1B variants causes lysis of wild-type cells
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-
additional information
?
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-
penicillin-binding protein 1b is the key enzyme responsible for the formation of the polysaccharide backbone of the peptidoglycan as well as for cross-linking of its peptide portion
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-
-
additional information
?
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-
dimerized enzyme synthesizes murein with long glycan strands of an average length of more than 25 disaccharide units with almost 50% of the peptides being part of cross-links. PBP1B is also capable of synthesizing trimeric muropeptide structures
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-
additional information
?
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-
penicillin binding protein 1b has transglycosylase and transpeptidase activity
-
-
-
additional information
?
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-
the penicillin-binding protein 1B is a bifunctional murein synthase containing both a transpeptidase domain and a transglycosylasedomain, The protein is present in three forms: alpha, beta and gamma
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-
-
additional information
?
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-
utility of Lipid II and Lipid IV substrates to probe the mechanism of the enzyme
-
-
-
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
-
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
-
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
-
additional information
?
-
-
PGT enzymes contain two substrate binding pockets flanking the enzymatic center. For a PGT enzyme in the process of extending the peptidoglycan chain, lipid II occupies the acceptor site, and the growing chain occupies the donor site and may extend through the enzyme's exit tunnel. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
-
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
-
additional information
?
-
-
PGT enzymes contain two substrate binding pockets flanking the enzymatic center. For a PGT enzyme in the process of extending the peptidoglycan chain, lipid II occupies the acceptor site, and the growing chain occupies the donor site and may extend through the enzyme's exit tunnel. Each round of catalysis results in the extension of the peptidoglycan chain by two saccharides and in the release of undecaprenyl diphosphate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
-
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
-
additional information
?
-
-
development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
-
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
-
additional information
?
-
-
positive cooperativity between acceptor and donor sites of the peptidoglycan glycosyltransferase, mechanism of interaction with substrates, overview. At low concentrations the disaccharide compounds bind selectively to the acceptor site and increase the affinity of the donor site to moenomycin A by heteroallosteric activation leading to an increased MtgA binding response
-
-
-
additional information
?
-
-
development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors
-
-
-
additional information
?
-
-
NMR and mass spectrometric analysis of enzyme-substrate binding
-
-
-
additional information
?
-
-
the enzyme possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity
-
-
-
additional information
?
-
-
the enzyme possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
additional information
?
-
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
peptidoglycan-synthetic enzyme activities of penicillin-binding protein 3 may by involved in the process of cell division
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
enzyme is involved in synthesis of peptidoglycan
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
PBP4 is dispensable and that, as in other bacteria, its absence can be compensated for by the second class A PBP, PBP1
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
gram-positive cocci have cell wall peptidoglycan which seems to be synthesized by penicillin-binding protein transpeptidases and a separate transglycosylase
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol

[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
-
i.e. lipid II
-
-
?
additional information

?
-
-
the enzyme is both an amidase and an endopeptidase. The enzyme is a lytic transglycosylase that degrades the glycan strands of the peptidoglycan into disaccharide units. The enzyme binds the cell wall, but only cleaves the glycan strands after the stem peptides have been removed. The enzyme alone is unable to cleave purified peptidoglycan but needs the presence of SpoIIP
-
-
-
additional information
?
-
-
overproduction of the inactive PBP1B variants causes lysis of wild-type cells
-
-
-
additional information
?
-
-
penicillin-binding protein 1b is the key enzyme responsible for the formation of the polysaccharide backbone of the peptidoglycan as well as for cross-linking of its peptide portion
-
-
-
additional information
?
-
-
lipid II, i.e. undecaprenyl-diphosphoryl-MurNAc(pentapeptide)-GlcNAc, is polymerized by the glycosyltransferase reaction, under the release of undecaprenol diphosphate
-
-
-
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(2R)-2-[[(2S)-2-([[(2R,3R,4R,5S,6R)-5-[[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy]-4-[(1S)-1-carboxyethoxy]-2-[[(hexadecyloxy)(hydroxy)phosphoryl]oxy]-6-(hydroxymethyl)oxan-3-yl]carbamoyl]amino)propanoyl]amino]pentanedioic acid
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3R,4R,5S,6R)-3-acetamido-2-([[(2R)-2-carboxy-2-(hexadecyloxy)ethoxy](hydroxy)phosphoryl]oxy)-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3R,4R,5S,6R)-3-acetamido-2-[[(hexadecyloxy)(hydroxy)phosphoryl]oxy]-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R,3S,4R,5R,6R)-3-[[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy]-5-(2-carboxyethyl)-6-([[(2R)-2-carboxy-2-(pentadecyloxy)ethoxy](hydroxy)phosphoryl]oxy)-2-(hydroxymethyl)oxan-4-yl]oxy]propanoyl]amino]propanoyl]amino]pentanedioic acid
-
-
(2R,3'R)-3-(3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato)-2-(3',7'-dimethyloctyloxy)propanoic acid
-
0.1 mM, 25% inhibition, 0.2 mM, 37% inhibition
(2R,3'R)-3-[3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato]-2-(3',7'-dimethyloctyloxy)propanoic acid
-
0.1 mM., 25% inhibition, 0.2 mM, 61% inhibition
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
(R)-3-((2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl)methylphosphinato)-2-octyloxypropanoic acid
-
0.1 mM, 17% inhibition
(R)-3-[3-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranosyl)propylphosphinato]-2-octyloxypropanoic acid
-
0.1 mM, 10% inhibition
(Z)-2-(2-acetamido-2-deoxy-alpha-D-glucopyranosyl)oxymethyl-3-tetradecylbutenedioic acid dilithium salt
-
0.1 mM, 28% inhibition
(Z)-2-farnesyl-3-methylbutenedioic acid dilithium salt
-
weak inhibition
(Z)-2-geranyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 12% inhibition
(Z)-2-nerolyl-3-methylbutenedioic acid dilithium salt
-
0.1 mM, 17% inhibition
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide
2-acetamido-3-O-[(1S)-1-carboxyethyl]-1-O-[[(2R)-2-carboxy-2-(hexadecyloxy)ethoxy](hydroxy)phosphoryl]-2-deoxy-alpha-D-glucopyranose
-
-
2-acetamido-4-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-3-O-[(1S)-1-carboxyethyl]-2-deoxy-1-O-[(hexadecyloxy)(hydroxy)phosphoryl]-alpha-D-glucopyranose
-
-
4-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-2-(carboxyamino)-3-O-[(1S)-1-carboxyethyl]-1-O-[[(2R)-2-carboxy-2-(pentadecyloxy)ethoxy](hydroxy)phosphoryl]-2-deoxy-alpha-D-glucopyranose
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
chaetomellic acid A dilithium salt
-
weak inhibition
chlorobiphenyl desleucyl vancomycin
chlorobiphenyl disaccharide
chlorobiphenyl vancomycin
Dimethylsulfoxide
-
in the presence of 0.05% N-lauroylsarcosine
neryl-moenomycin A
active site inhibitor
Sodium 1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid
-
in the absence of detergents, stimulates in the presence of high concentrations of methanol and detergents
sodium deoxycholate
-
in the presence of methanol, inhibits at 0.5%
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate

-
-
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
-
-
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
-
-
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
-
-
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one

-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one

-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide

-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide

-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus with MIC values of 0.024 and 0.048 mg/ml, respectively
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(m-tolyl)acetamide
-
an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus with MIC values of 0.024 and 0.048 mg/ml, respectively
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid

-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol

-
-
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
-
-
AC326-alpha

-
-
ACL19098

-
-
ACL19109

-
-
ACL19110

-
-
ACL19243

-
-
ACL19273

-
-
ACL19336

-
-
chlorobiphenyl desleucyl vancomycin

-
-
chlorobiphenyl desleucyl vancomycin
-
-
chlorobiphenyl desleucyl vancomycin
-
-
chlorobiphenyl desleucyl vancomycin
-
-
chlorobiphenyl desleucyl vancomycin
-
-
chlorobiphenyl disaccharide

-
-
chlorobiphenyl disaccharide
-
-
chlorobiphenyl disaccharide
-
-
chlorobiphenyl disaccharide
-
-
chlorobiphenyl disaccharide
-
-
chlorobiphenyl vancomycin

-
-
chlorobiphenyl vancomycin
-
-
chlorobiphenyl vancomycin
-
-
chlorobiphenyl vancomycin
-
-
chlorobiphenyl vancomycin
-
-
EDTA

-
in the absence of detergents, stimulates in the presence of high concentrations of methanol and detergents
EDTA
-
the enzyme is almost inactive in presence of EDTA
Garneau-5

-
-
HTS6

-
-
HTS7

-
-
HTS8

-
-
Macarbomycin

-
-
-
mersacidin

-
a lantibiotic
-
mersacidin
-
a lantibiotic
-
Moenomycin

-
re-docking of the inhibitor
Moenomycin
-
coupled transglycosylasetranspeptidase
Moenomycin
-
no inhibition
Moenomycin
-
75 nM, 50% inhibition
Moenomycin
-
moenomycin A inhibits the transglycosylation step by binding to the donor site of the glycosyltransferase
Moenomycin
-
re-docking of the inhibitor
moenomycin A

active site inhibitor
moenomycin A
-
; moenomycins are phosphoglycolipid antibiotics that directly bind to PGT enzymes. Moenomycins are produced by certain Streptomyces species as a complex of related compounds in which moenomycin A is the major form
moenomycin A
-
; moenomycins are phosphoglycolipid antibiotics that directly bind to PGT enzymes. Moenomycins are produced by certain Streptomyces species as a complex of related compounds in which moenomycin A is the major form
moenomycin disaccharide

-
-
moenomycin disaccharide
-
-
moenomycin disaccharide
-
-
moenomycin disaccharide
-
-
moenomycin disaccharide
-
-
moenomycin trisaccharide

-
-
moenomycin trisaccharide
-
-
moenomycin trisaccharide
-
-
moenomycin trisaccharide
-
-
moenomycin trisaccharide
-
-
penicillin

-
coupled transglycosylasetranspeptidase
Triton X-100

-
inhibits at 0.1%
Triton X-100
-
up to 0.6%
TS30153

-
-
Vancomycin

-
-
Vancomycin
-
; a glycopeptide
Vancomycin
-
; a glycopeptide
additional information

-
synthesis of diverse isatin derivatives, MIC values for activity against Gram-positive Bacillus subtilis and Staphylococcus aureus, most compounds are poorly active, overview
-
additional information
-
molecular docking and modelling study using the structure of PBP1b, PDB ID 3VMA. NMR and mass spectrometric analysis of enzyme-inhibitor binding; PGT enzymes can be inhibited directly by compounds binding to the enzyme and indirectly by compounds binding to the lipid II substrate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors. Design of a library of disaccharide compounds based on the minimum moenomycin fragment with peptidoglycan glycosyltransferase inhibitory activity and based on a more drug-like and synthetically versatile disaccharide building block. A subset of these disaccharide compounds bind and inhibit the glycosyltransferase enzyme. Inhibitor-enzyme binding structure analysis by 1H NMR spectral data and using crystal structure PDB ID 3VMA. MIC values with strain imp mutant BAS849
-
additional information
-
several analogues of the enzyme's lipid II substrate are synthesized previously and found to inhibit the enzyme activity in vitro and cause bacterial growth defect, overview
-
additional information
-
synthesis of diverse isatin derivatives, MIC values for activity against Gram-positive Bacillus subtilis and Staphylococcus aureus, most compounds are poorly active, overview
-
additional information
-
molecular docking and modelling study using the structure of MGT, PDB ID 3HZS. NMR and mass spectrometric analysis of enzyme-inhibitor binding. IC50 Inhibitory curves for MGT against moenomycin complex and vancomycin, overview; PGT enzymes can be inhibited directly by compounds binding to the enzyme and indirectly by compounds binding to the lipid II substrate. Development of glycosyltransferase enzymatic activity and binding assays using the natural products moenomycin and vancomycin as model inhibitors. Design of a library of disaccharide compounds based on the minimum moenomycin fragment with peptidoglycan glycosyltransferase inhibitory activity and based on a more drug-like and synthetically versatile disaccharide building block. A subset of these disaccharide compounds bind and inhibit the glycosyltransferase enzyme. Inhibitor-enzyme binding structure analysis by 1H NMR spectral data and using crystal structure PDB ID 3HZS. MIC values with strain ATCC 29213
-
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0.0098
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
Escherichia coli
-
-
0.034
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
Helicobacter pylori
-
-
0.0037
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
Helicobacter pylori
-
-
0.0093
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
Helicobacter pylori
-
-
0.0497 - 0.0732
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
0.00388
chlorobiphenyl desleucyl vancomycin
0.0015
chlorobiphenyl vancomycin
0.000006 - 0.019
moenomycin A
0.000033
moenomycin disaccharide
0.000016
moenomycin trisaccharide
0.00038 - 0.000685
Vancomycin
0.0497
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol

Escherichia coli
-
pH 7.5, 25°C, PBP1b
0.0732
4-[3-amino-3-([1,1'-biphenyl]-4-yl)propanamido]-1,5-anhydro-2,4-dideoxy-3-O-[2-deoxy-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-beta-D-glucopyranosyl]-2-({[3-(trifluoromethyl)phenyl]carbamoyl}amino)-D-galactitol
Staphylococcus aureus
-
pH 7.5, 25°C, MGT
0.0062
ACL19098

Escherichia coli
-
pH 7.5, 25°C; pH 7.5, 25°C, PBP1b
0.0073
ACL19098
Staphylococcus aureus
-
pH 7.5, 25°C, MGT; pH 8.0, 20°C
0.0346
ACL19109

Escherichia coli
-
pH 7.5, 25°C; pH 7.5, 25°C, PBP1b
0.0382
ACL19109
Staphylococcus aureus
-
pH 7.5, 25°C, MGT; pH 8.0, 20°C
0.0365
ACL19110

Escherichia coli
-
pH 7.5, 25°C; pH 7.5, 25°C, PBP1b
0.0905
ACL19110
Staphylococcus aureus
-
pH 7.5, 25°C, MGT; pH 8.0, 20°C
0.0497
ACL19243

Escherichia coli
-
pH 7.5, 25°C
0.0732
ACL19243
Staphylococcus aureus
-
pH 8.0, 20°C
0.04
ACL19273

Escherichia coli
-
pH 7.5, 25°C; pH 7.5, 25°C, PBP1b
0.05
ACL19273
Staphylococcus aureus
-
pH 7.5, 25°C, MGT; pH 8.0, 20°C
0.0362
ACL19336

Escherichia coli
-
pH 7.5, 25°C; pH 7.5, 25°C, PBP1b
0.075
ACL19336
Staphylococcus aureus
-
pH 7.5, 25°C, MGT; pH 8.0, 20°C
0.00388
chlorobiphenyl desleucyl vancomycin

Aquifex aeolicus
-
-
0.00388
chlorobiphenyl desleucyl vancomycin
Escherichia coli
-
-
0.0015
chlorobiphenyl vancomycin

Aquifex aeolicus
-
-
0.0015
chlorobiphenyl vancomycin
Escherichia coli
-
-
0.000006
moenomycin A

Aquifex aeolicus
-
-
0.000006
moenomycin A
Escherichia coli
-
-
0.0000076
moenomycin A
Staphylococcus aureus
-
pH 8.0, 20°C
0.019
moenomycin A
Escherichia coli
-
pH 7.5, 25°C
0.000033
moenomycin disaccharide

Aquifex aeolicus
-
-
0.000033
moenomycin disaccharide
Escherichia coli
-
-
0.000016
moenomycin trisaccharide

Aquifex aeolicus
-
-
0.000016
moenomycin trisaccharide
Escherichia coli
-
-
0.00038
Vancomycin

Aquifex aeolicus
-
-
0.00038
Vancomycin
Escherichia coli
-
-
0.00054
Vancomycin
Escherichia coli
-
pH 7.5, 25°C
0.000685
Vancomycin
Staphylococcus aureus
-
pH 8.0, 20°C
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E83A
mutant with undetectable activity
K124A
mutant shows 5fold reduced activity compared to the wild type enzyme
K137A
mutant with undetectable activity
Q121A
mutant with undetectable activity
R132A
mutant with barely detectable activity (about 3% of wild type)
S116A
mutant shows 10fold reduced activity compared to the wild type enzyme
E78A
-
the mutant shows 89% sporulation efficiency compared to the wild type enzyme
E88A
-
the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
E96A
-
the mutant shows wild type sporulation efficiency
H297A
-
the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
K99A
-
the mutant shows wild type sporulation efficiency
Q101A
-
the mutant shows 89% sporulation efficiency compared to the wild type enzyme
Q303A
-
the mutant shows 88% sporulation efficiency compared to the wild type enzyme
R106A
-
the mutant is severely impaired in sporulation efficiency (0.05% efficiency compared to the wild type enzyme)
R269A
-
the mutant shows 86% sporulation efficiency compared to the wild type enzyme
S276A
-
the mutant shows 93% sporulation efficiency compared to the wild type enzyme
T164A
-
the mutant shows 73% sporulation efficiency compared to the wild type enzyme
T188A
-
the mutant shows 33% sporulation efficiency compared to the wild type enzyme
Y171A
-
the mutant shows 71% sporulation efficiency compared to the wild type enzyme
Y201A
-
the mutant shows 87% sporulation efficiency compared to the wild type enzyme
Y323A
-
the mutant is severely impaired in sporulation efficiency (0.01% efficiency compared to the wild type enzyme)
Y324A
-
the mutant is severely impaired in sporulation efficiency (0.02% efficiency compared to the wild type enzyme)
Y80A
-
the mutant shows 70% sporulation efficiency compared to the wild type enzyme
D234N
-
the mutant shows 14% of wild type activity
E290Q
-
the mutant shows 2% of wild type activity
F237A
-
mutant with completely abolished activity; no activity in vitro
G242A
-
the mutant shows 4% of wild type activity
G264L
-
no activity in vitro
H240A
-
mutant with completely abolished activity
H240Q
-
the mutant shows 7% of wild type activity
K274A
-
no activity in vitro
K287A
-
the mutant shows 63% of wild type activity
N312A
-
mutant with completely abolished activity
Q271A
-
no activity in vitro
R372A
-
the mutant shows 19% of wild type activity
S266A
-
the mutant displays 11% of wild type activity
T267A
-
no activity in vitro
Y310F
-
no activity in vitro
N526K
-
the mutant shows decreased susceptibility toward ampicillin and amoxicillin
F104A
-
site-directed mutagenesis, the binding response for F104A is drastically decreased compared to the wild-type
F120S
-
site-directed mutagenesis, modification of the residue within the hydrophobic region of enzyme MtgA yields monodisperse forms of the protein with apparently no change in its secondary structure content, but at the expense of the enzyme function. Mutation F120S may affect the outer helix transition/conformational change during catalysis
F150S
-
site-directed mutagenesis, insoluble mutant
F158S
-
site-directed mutagenesis
L112N
-
site-directed mutagenesis
L119N
-
site-directed mutagenesis, modification of the residue within the hydrophobic region of enzyme MtgA yields monodisperse forms of the protein with apparently no change in its secondary structure content, but at the expense of the enzyme function. Mutation L119N may affect the outer helix transition/conformational change during catalysis
L119N/F120S/E100Q
-
structure of MtgA in complex with moenomycin A bound to the donor site, PDB 3HZS
V154S
-
site-directed mutagenesis
E233Q

-
mutation inactivates the transglycosylase domain
E233Q
-
the mutant shows 0.2% of wild type activity
E100Q

-
mutant of the soluble form of Staphylococcus aureus MGT devoid of its membrane anchor, called SauH6-MGT. glycosyltransferase activity of the mutant is reduced 500fold compared to the wild type
E100Q
-
site-directed mutagenesis, E100Q binds moenomycin A in the same order of magnitude as the wild-type
additional information

-
ponA is synthesized with the addition of ribosome binding site (AGGAGGT) and linker (AAAACAT) upstream of the Met1 codon. This construct is inserted at the XbaI and HindIII sites of pACT3 (21), generating pMCC1, with PBP1a expression under control of the tac promoter. pMCC1 and pACT3 are transformed into hyperpermeable Escherichia coli isolate generating CBS-3546 and CBS-3567, respectively
additional information
-
ponA is synthesized with the addition of ribosome binding site (AGGAGGT) and linker (AAAACAT) upstream of the Met1 codon. This construct is inserted at the XbaI and HindIII sites of pACT3 (21), generating pMCC1, with PBP1a expression under control of the tac promoter. pMCC1 and pACT3 are transformed into hyperpermeable Escherichia coli isolate generating CBS-3546 and CBS-3567, respectively
-
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Taku, A.; Stuckey, M.; Fan, D.P.
Purification of the peptidoglycan transglycosylase of Bacillus megaterium
J. Biol. Chem.
257
5018-5022
1982
Bacillus megaterium, Bacillus megaterium 899
brenda
Ishino, F.; Matsuhashi, M.
Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence
Biochem. Biophys. Res. Commun.
101
905-911
1981
Escherichia coli
brenda
Park, W.; Matsuhashi, M.
Staphylococcus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins
J. Bacteriol.
157
538-544
1984
Micrococcus luteus, Micrococcus luteus SM1, Staphylococcus aureus, Staphylococcus aureus SAK 101
brenda
Nakagawa, J.; Tamaki, S.; Tomioka, S.; Matsuhashi, M.
Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. Penicillin-binding protein 1Bs of Escherichia coli with activities of transglycosylase and transpeptidase
J. Biol. Chem.
259
13937-13946
1984
Escherichia coli, Escherichia coli JA200/pLC19-19
brenda
Park, W.; Seto, H.; Hakenbeck, R.; Matsuhashi, M.
Major peptidoglycan transglycosylase activity in Streptococcus pneumoniae that is not a penicillin-binding protein
FEMS Microbiol. Lett.
27
45-48
1985
Escherichia coli, Streptococcus pneumoniae, Streptococcus pneumoniae R6cwl
-
brenda
Van Heijenoort, J.
Formation of the glycan chains in the synthesis of bacterial peptidoglycan
Glycobiology
11
25R-36R
2001
Escherichia coli, Streptococcus pneumoniae
brenda
Chandrakala, B.; Shandil, R.K.; Mehra, U.; Ravishankar, S.; Kaur, P.; Usha, V.; Joe, B.; deSousa, S.M.
High-throughput screen for inhibitors of transglycosylase and/or transpeptidase activities of Escherichia coli penicillin binding protein 1b
Antimicrob. Agents Chemother.
48
30-40
2004
Escherichia coli
brenda
Stefanova, M.E.; Tomberg, J.; Olesky, M.; Holtje, J.V.; Gutheil, W.G.; Nicholas, R.A.
Neisseria gonorrhoeae penicillin-binding protein 3 exhibits exceptionally high carboxypeptidase and beta-lactam binding activities
Biochemistry
42
14614-14625
2003
Neisseria gonorrhoeae, Neisseria gonorrhoeae (O85665)
brenda
Barrett, D.S.; Chen, L.; Litterman, N.K.; Walker, S.
Expression and characterization of the isolated glycosyltransferase module of Escherichia coli PBP1b
Biochemistry
43
12375-12381
2004
Escherichia coli
brenda
Garneau, S.; Qiao, L.; Chen, L.; Walker, S.; Vederas, J.C.
Synthesis of mono- and disaccharide analogs of moenomycin and lipid II for inhibition of transglycosylase activity of penicillin-binding protein 1b
Bioorg. Med. Chem.
12
6473-6494
2004
Escherichia coli
brenda
Meisel, U.; Holtje, J.V.; Vollmer, W.
Overproduction of inactive variants of the murein synthase PBP1B causes lysis in Escherichia coli
J. Bacteriol.
185
5342-5348
2003
Escherichia coli
brenda
Bertsche, U.; Breukink, E.; Kast, T.; Vollmer, W.
In vitro murein (peptidoglycan) synthesis by dimers of the bifunctional transglycosylase-transpeptidase PBP1B from Escherichia coli
J. Biol. Chem.
280
38096-38101
2005
Escherichia coli
brenda
Terrak, M.; Ghosh, T.G.; van Heijenoort, J.; et al.
The catalytic, glycosyl transferase and acyl transferase modules of the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b of Escherichia coli
Mol. Microbiol.
34
350-364
1999
Escherichia coli
brenda
Ramachandran, V.; Chandrakala, B.; Kumar, V.P.; Usha, V.; Solapure, S.M.; de Sousa, S.M.
Screen for inhibitors of the coupled transglycosylase-transpeptidase of peptidoglycan biosynthesis in Escherichia coli
Antimicrob. Agents Chemother.
50
1425-1432
2006
Escherichia coli
brenda
Fraipont, C.; Sapunaric, F.; Zervosen, A.; Auger, G.; Devreese, B.; Lioux, T.; Blanot, D.; Mengin-Lecreulx, D.; Herdewijn, P.; van Beeumen, J.; Frere, J.M.; Nguyen-Disteche, M.
Glycosyl transferase activity of the Escherichia coli penicillin-binding protein 1b: specificity profile for the substrate
Biochemistry
45
4007-4013
2006
Escherichia coli
brenda
Offant, J.; Michoux, F.; Dermiaux, A.; Biton, J.; Bourne, Y.
Functional characterization of the glycosyltransferase domain of penicillin-binding protein 1a from Thermotoga maritima
Biochim. Biophys. Acta
1764
1036-1042
2006
Thermotoga maritima (Q9WZY8), Thermotoga maritima
brenda
Zhang, Y.; Fechter, E.J.; Wang, T.A.; Barrett, D.; Walker, S.; Kahne, D.E.
Synthesis of heptaprenyl-lipid IV to analyze peptidoglycan glycosyltransferases
J. Am. Chem. Soc.
129
3080-3081
2007
Escherichia coli
brenda
Zawadzka-Skomial, J.; Markiewicz, Z.; Nguyen-Disteche, M.; Devreese, B.; Frere, J.M.; Terrak, M.
Characterization of the bifunctional glycosyltransferase/acyltransferase penicillin-binding protein 4 of Listeria monocytogenes
J. Bacteriol.
188
1875-1881
2006
Listeria monocytogenes
brenda
Terrak, M.; Nguyen-Disteche, M.
Kinetic characterization of the monofunctional glycosyltransferase from Staphylococcus aureus
J. Bacteriol.
188
2528-2532
2006
Staphylococcus aureus
brenda
Yuan, Y.; Barrett, D.; Zhang, Y.; Kahne, D.; Sliz, P.; Walker, S.
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis
Proc. Natl. Acad. Sci. USA
104
5348-5353
2007
Aquifex aeolicus
brenda
Yuan, Y.; Fuse, S.; Ostash, B.; Sliz, P.; Kahne, D.; Walker, S.
Structural analysis of the contacts anchoring moenomycin to peptidoglycan glycosyltransferases and implications for antibiotic design
ACS Chem. Biol.
3
429-436
2008
Aquifex aeolicus (O66874)
brenda
Terrak, M.
Peptidoglycan glycosyltransferase inhibition: New perspectives for an old target
Anti-Infect. Agents Med. Chem.
7
180-192
2008
Aquifex aeolicus, Enterococcus faecalis, Escherichia coli, Escherichia coli BAS849, Helicobacter pylori, Staphylococcus aureus
-
brenda
Izdebski, R.; Rutschmann, J.; Fiett, J.; Sadowy, E.; Gniadkowski, M.; Hryniewicz, W.; Hakenbeck, R.
Highly variable penicillin resistance determinants PBP 2x, PBP 2b, and PBP 1a in isolates of two Streptococcus pneumoniae clonal groups, Poland23F-16 and Poland6B-20
Antimicrob. Agents Chemother.
52
1021-1027
2008
Streptococcus pneumoniae (P0A3M5), Streptococcus pneumoniae (P14677), Streptococcus pneumoniae (Q4TUQ8), Streptococcus pneumoniae
brenda
Lovering, A.L.; Gretes, M.; Strynadka, N.C.
Structural details of the glycosyltransferase step of peptidoglycan assembly
Curr. Opin. Struct. Biol.
18
534-543
2008
Aquifex aeolicus, Bacillus subtilis, Caulobacter vibrioides, Escherichia coli, Mycobacterium tuberculosis, Rhodobacter sphaeroides, Staphylococcus aureus
brenda
Shuel, M.L.; Tsang, R.S.
Canadian beta-lactamase-negative Haemophilus influenzae isolates showing decreased susceptibility toward ampicillin have significant penicillin binding protein 3 mutations
Diagn. Microbiol. Infect. Dis.
63
379-383
2009
Haemophilus influenzae
brenda
Wang, T.S.; Manning, S.A.; Walker, S.; Kahne, D.
Isolated peptidoglycan glycosyltransferases from different organisms produce different glycan chain lengths
J. Am. Chem. Soc.
130
14068-14069
2008
Enterococcus faecalis, Escherichia coli, Staphylococcus aureus
brenda
Perlstein, D.; Wang, T.; Doud, E.; Kahne, D.; Walker, S.
The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases
J. Am. Chem. Soc.
132
48-49
2010
Aquifex aeolicus
brenda
Derouaux, A.; Wolf, B.; Fraipont, C.; Breukink, E.; Nguyen-Disteche, M.; Terrak, M.
The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN
J. Bacteriol.
190
1831-1834
2008
Escherichia coli
brenda
Terrak, M.; Sauvage, E.; Derouaux, A.; Dehareng, D.; Bouhss, A.; Breukink, E.; Jeanjean, S.; Nguyen-Disteche, M.
Importance of the conserved residues in the peptidoglycan glycosyltransferase module of the class A penicillin-binding protein 1b of Escherichia coli
J. Biol. Chem.
283
28464-28470
2008
Escherichia coli
brenda
Lovering, A.L.; De Castro, L.; Strynadka, N.C.
Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer
J. Mol. Biol.
383
167-177
2008
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
brenda
Sung, M.T.; Lai, Y.T.; Huang, C.Y.; Chou, L.Y.; Shih, H.W.; Cheng, W.C.; Wong, C.H.; Ma, C.
Crystal structure of the membrane-bound bifunctional transglycosylase PBP1b from Escherichia coli
Proc. Natl. Acad. Sci. USA
106
8824-8829
2009
Escherichia coli (P02919)
brenda
Bandara, A.; Schurig, G.; Sriranganathan, N.; Prasad, R.; Boyle, S.
The putative penicillin-binding proteins 1 and 2 are important for viability, growth and cell morphology of Brucella melitensis
Vet. Microbiol.
133
387-393
2009
Brucella melitensis
brenda
Morlot, C.; Uehara, T.; Marquis, K.; Bernhardt, T.; Rudner, D.
A highly coordinated cell wall degradation machine governs spore morphogenesis in Bacillus subtilis
Genes Dev.
24
411-422
2010
Bacillus subtilis
brenda
de Leon, S.R.; Daniels, K.; Clarke, A.J.
Production and purification of the penicillin-binding protein 3 from Pseudomonas aeruginosa
Protein Expr. Purif.
73
177-183
2010
Pseudomonas aeruginosa (G3XD46), Pseudomonas aeruginosa
brenda
Bury, D.; Dahmane, I.; Derouaux, A.; Dumbre, S.; Herdewijn, P.; Matagne, A.; Breukink, E.; Mueller-Seitz, E.; Petz, M.; Terrak, M.
Positive cooperativity between acceptor and donor sites of the peptidoglycan glycosyltransferase
Biochem. Pharmacol.
93
141-150
2015
Staphylococcus aureus
brenda
Wang, Y.; Chan, F.Y.; Sun, N.; Lui, H.K.; So, P.K.; Yan, S.C.; Chan, K.F.; Chiou, J.; Chen, S.; Abagyan, R.; Leung, Y.C.; Wong, K.Y.
Structure-based design, synthesis, and biological evaluation of isatin derivatives as potential glycosyltransferase inhibitors
Chem. Biol. Drug Des.
84
685-696
2014
Bacillus subtilis, Staphylococcus aureus, Staphylococcus aureus ATCC 29213
brenda
Mesleh, M.F.; Rajaratnam, P.; Conrad, M.; Chandrasekaran, V.; Liu, C.M.; Pandya, B.A.; Hwang, Y.S.; Rye, P.T.; Muldoon, C.; Becker, B.; Zuegg, J.; Meutermans, W.; Moy, T.I.
Targeting bacterial cell wall peptidoglycan synthesis by inhibition of glycosyltransferase activity
Chem. Biol. Drug Des.
87
190-199
2016
Escherichia coli, Escherichia coli imp, Staphylococcus aureus, Staphylococcus aureus ATCC 29213
brenda
Egan, A.J.; Biboy, J.; vant Veer, I.; Breukink, E.; Vollmer, W.
Activities and regulation of peptidoglycan synthases
Philos. Trans. R. Soc. Lond. B Biol. Sci.
370
0000
2015
Escherichia coli (P02919)
brenda