FEMS Microbiology Reviews, ISSN 0168-6445, 03/2008, Volume 32, Issue 2, pp. 234 - 258
Penicillin‐binding proteins (PBPs) have been scrutinized for over 40 years. Recent structural information on PBPs together with the ongoing long‐term...
3D structure | transpeptidase | penicillin‐binding | transglycosylase | peptidoglycan synthesis | Peptidoglycan synthesis | Transglycosylase | Penicillin-binding | Transpeptidase | BETA-LACTAM RESISTANCE | ACYL-ENZYME COMPLEX | ESCHERICHIA-COLI | penicillin-binding | ALA-PEPTIDASE REVEALS | MICROBIOLOGY | PREDICTED SECONDARY STRUCTURES | ENTEROCOCCUS-FAECIUM BM4339 | STREPTOCOCCUS-PNEUMONIAE | BACILLUS-SUBTILIS | ALANINE CARBOXYPEPTIDASE IA | CELL-WALL PEPTIDOGLYCAN | Protein Structure, Tertiary | Bacteria - metabolism | Peptidyl Transferases - metabolism | Bacteria - chemistry | Multienzyme Complexes - classification | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Glycosyltransferases - chemistry | Penicillin-Binding Proteins - classification | Peptidyl Transferases - chemistry | Bacterial Proteins - chemistry | Multienzyme Complexes - metabolism | Penicillin-Binding Proteins - metabolism | Peptide Hydrolases - chemistry | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Penicillin-Binding Proteins - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | beta-Lactamases - metabolism | Peptide Hydrolases - metabolism | Physiological aspects | Peptidoglycans
3D structure | transpeptidase | penicillin‐binding | transglycosylase | peptidoglycan synthesis | Peptidoglycan synthesis | Transglycosylase | Penicillin-binding | Transpeptidase | BETA-LACTAM RESISTANCE | ACYL-ENZYME COMPLEX | ESCHERICHIA-COLI | penicillin-binding | ALA-PEPTIDASE REVEALS | MICROBIOLOGY | PREDICTED SECONDARY STRUCTURES | ENTEROCOCCUS-FAECIUM BM4339 | STREPTOCOCCUS-PNEUMONIAE | BACILLUS-SUBTILIS | ALANINE CARBOXYPEPTIDASE IA | CELL-WALL PEPTIDOGLYCAN | Protein Structure, Tertiary | Bacteria - metabolism | Peptidyl Transferases - metabolism | Bacteria - chemistry | Multienzyme Complexes - classification | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Glycosyltransferases - chemistry | Penicillin-Binding Proteins - classification | Peptidyl Transferases - chemistry | Bacterial Proteins - chemistry | Multienzyme Complexes - metabolism | Penicillin-Binding Proteins - metabolism | Peptide Hydrolases - chemistry | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Glycosyltransferases - metabolism | beta-Lactams - pharmacology | Penicillin-Binding Proteins - chemistry | Bacterial Proteins - metabolism | Bacterial Proteins - classification | beta-Lactamases - metabolism | Peptide Hydrolases - metabolism | Physiological aspects | Peptidoglycans
Journal Article
Nature, ISSN 0028-0836, 08/2016, Volume 537, Issue 7622, pp. 634 - 638
Elongation of rod-shaped bacteria is mediated by a dynamic peptidoglycan-synthetizing machinery called the Rod complex. Here we report that, in Bacillus...
BETA-LACTAM RESISTANCE | GENE | BACILLUS-SUBTILIS | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | PENICILLIN-BINDING PROTEINS | DYNAMICS | FLIPPASE | PEPTIDOGLYCAN SYNTHESIS | PRECURSORS | DIVISION | Peptidoglycan Glycosyltransferase - metabolism | Bacillus subtilis - cytology | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Polymerization | Penicillin-Binding Proteins - genetics | Bacillus subtilis - enzymology | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Oligosaccharides - pharmacology | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | Phenotype | Bacillus subtilis - growth & development | Cell Division | Cell Wall - metabolism | Drug Design | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Drug Resistance, Bacterial - drug effects | Mutation | Bacillus subtilis - drug effects | Physiological aspects | Bacillus subtilis | Bacterial cell walls | Proteins | Antigens | Enzymes | Bacterial infections | Peptides | Penicillin | Bacteria | Lipids | Biosynthesis
BETA-LACTAM RESISTANCE | GENE | BACILLUS-SUBTILIS | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | PENICILLIN-BINDING PROTEINS | DYNAMICS | FLIPPASE | PEPTIDOGLYCAN SYNTHESIS | PRECURSORS | DIVISION | Peptidoglycan Glycosyltransferase - metabolism | Bacillus subtilis - cytology | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Polymerization | Penicillin-Binding Proteins - genetics | Bacillus subtilis - enzymology | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Oligosaccharides - pharmacology | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | Phenotype | Bacillus subtilis - growth & development | Cell Division | Cell Wall - metabolism | Drug Design | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Drug Resistance, Bacterial - drug effects | Mutation | Bacillus subtilis - drug effects | Physiological aspects | Bacillus subtilis | Bacterial cell walls | Proteins | Antigens | Enzymes | Bacterial infections | Peptides | Penicillin | Bacteria | Lipids | Biosynthesis
Journal Article
Biochimie, ISSN 0300-9084, 09/2018, Volume 152, pp. 1 - 5
Peptidoglycan glycosyltransferases (GTase) of family 51 are essential enzymes for the synthesis of the glycan chains of the bacterial cell wall. They are...
Peptidoglycan | Moenomycin | Lipid II | Glycosyltransferase | Fluorescence assay | CRYSTAL-STRUCTURE | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | STAPHYLOCOCCUS-AUREUS | PROTEINS | TRANSGLYCOSYLATION STEP | Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives | Staphylococcus aureus - enzymology | Mutagenesis, Site-Directed | Peptidoglycan Glycosyltransferase - metabolism | Electrophoresis, Polyacrylamide Gel | Tryptophan - genetics | Enzyme Inhibitors - pharmacology | Spectrometry, Fluorescence | Substrate Specificity | Tryptophan - metabolism | Peptidoglycan Glycosyltransferase - genetics | Uridine Diphosphate N-Acetylmuramic Acid - metabolism | Bambermycins - metabolism | High-Throughput Screening Assays | Protein Binding | Ligands | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Circular Dichroism
Peptidoglycan | Moenomycin | Lipid II | Glycosyltransferase | Fluorescence assay | CRYSTAL-STRUCTURE | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | STAPHYLOCOCCUS-AUREUS | PROTEINS | TRANSGLYCOSYLATION STEP | Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives | Staphylococcus aureus - enzymology | Mutagenesis, Site-Directed | Peptidoglycan Glycosyltransferase - metabolism | Electrophoresis, Polyacrylamide Gel | Tryptophan - genetics | Enzyme Inhibitors - pharmacology | Spectrometry, Fluorescence | Substrate Specificity | Tryptophan - metabolism | Peptidoglycan Glycosyltransferase - genetics | Uridine Diphosphate N-Acetylmuramic Acid - metabolism | Bambermycins - metabolism | High-Throughput Screening Assays | Protein Binding | Ligands | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Circular Dichroism
Journal Article
Journal of Bacteriology, ISSN 0021-9193, 2017, Volume 199, Issue 7
Peptidoglycan is a vital component of nearly all cell wall-bearing bacteria and is a valuable target for antibacterial therapy. However, despite decades of...
PBP1A | Peptidoglycan | PBP1B | Spheroplast | Bacterial morphology | bacterial morphology | spheroplast | PEPTIDOGLYCAN SYNTHASE PBP1B | D-AMINO ACIDS | MICROBIOLOGY | CELL WALL POLYMERASES | L-FORMS | DIVISION | peptidoglycan | SHAPE | GRAM-NEGATIVE BACTERIA | Z-RING | PENICILLIN-BINDING PROTEINS | UNDECAPRENYL PHOSPHATE | Cell Proliferation | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - genetics | Escherichia coli - cytology | Gene Expression Regulation, Enzymologic - physiology | Penicillin-Binding Proteins - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - genetics | Gene Expression Regulation, Bacterial - physiology | Peptidoglycan Glycosyltransferase - genetics | Escherichia coli Proteins - genetics | Mutation | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | Spheroplasts - physiology | Research | Escherichia coli | Glycosyltransferases | Peptidyl transferases
PBP1A | Peptidoglycan | PBP1B | Spheroplast | Bacterial morphology | bacterial morphology | spheroplast | PEPTIDOGLYCAN SYNTHASE PBP1B | D-AMINO ACIDS | MICROBIOLOGY | CELL WALL POLYMERASES | L-FORMS | DIVISION | peptidoglycan | SHAPE | GRAM-NEGATIVE BACTERIA | Z-RING | PENICILLIN-BINDING PROTEINS | UNDECAPRENYL PHOSPHATE | Cell Proliferation | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - genetics | Escherichia coli - cytology | Gene Expression Regulation, Enzymologic - physiology | Penicillin-Binding Proteins - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - genetics | Gene Expression Regulation, Bacterial - physiology | Peptidoglycan Glycosyltransferase - genetics | Escherichia coli Proteins - genetics | Mutation | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | Spheroplasts - physiology | Research | Escherichia coli | Glycosyltransferases | Peptidyl transferases
Journal Article
Philosophical transactions / Royal Society of London. Biological sciences, ISSN 0962-8436, 10/2015, Volume 370, Issue 1679, pp. 20150031 - 20150031
Peptidoglycan (PG) is an essential component in the cell wall of nearly all bacteria, forming a continuous, mesh-like structure, called the sacculus, around...
Peptidoglycan | Penicillin-binding protein | Glycosyltransferase | Agricultural and Biological Sciences(all) | Lipid II | Carboxypeptidase | Biochemistry, Genetics and Molecular Biology(all) | Transpeptidase | transpeptidase | BACTERIAL CELL WALLS | ESCHERICHIA-COLI | penicillin-binding protein | DD-CARBOXYPEPTIDASE-TRANSPEPTIDASE | PEPTIDE CROSS-LINKING | IN-VITRO SYNTHESIS | KINETIC CHARACTERIZATION | carboxypeptidase | peptidoglycan | lipid II | glycosyltransferase | LIPID-II | BIOLOGY | STAPHYLOCOCCUS-AUREUS | NEWLY SYNTHESIZED PEPTIDOGLYCAN | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Peptidoglycan - chemistry | Models, Molecular | Substrate Specificity | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - metabolism | Escherichia coli Proteins - classification | Peptidoglycan - biosynthesis | Penicillin-Binding Proteins - chemistry | Escherichia coli - metabolism | Kinetics | Escherichia coli Proteins - chemistry | 200 | 1001 | Review
Peptidoglycan | Penicillin-binding protein | Glycosyltransferase | Agricultural and Biological Sciences(all) | Lipid II | Carboxypeptidase | Biochemistry, Genetics and Molecular Biology(all) | Transpeptidase | transpeptidase | BACTERIAL CELL WALLS | ESCHERICHIA-COLI | penicillin-binding protein | DD-CARBOXYPEPTIDASE-TRANSPEPTIDASE | PEPTIDE CROSS-LINKING | IN-VITRO SYNTHESIS | KINETIC CHARACTERIZATION | carboxypeptidase | peptidoglycan | lipid II | glycosyltransferase | LIPID-II | BIOLOGY | STAPHYLOCOCCUS-AUREUS | NEWLY SYNTHESIZED PEPTIDOGLYCAN | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Penicillin-Binding Proteins - classification | Peptidoglycan - chemistry | Models, Molecular | Substrate Specificity | Escherichia coli Proteins - metabolism | Penicillin-Binding Proteins - metabolism | Escherichia coli Proteins - classification | Peptidoglycan - biosynthesis | Penicillin-Binding Proteins - chemistry | Escherichia coli - metabolism | Kinetics | Escherichia coli Proteins - chemistry | 200 | 1001 | Review
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2014, Volume 136, Issue 24, pp. 8492 - 8495
Glycosyltransferases that act on polyprenol pyrophosphate substrates are challenging to study because their lipid-linked substrates are difficult to isolate...
MYCOBACTERIUM-TUBERCULOSIS | ARABINOGALACTAN | PEPTIDOGLYCAN | LENGTH CONTROL | MECHANISM | N-LINKED GLYCOSYLATION | BIOSYNTHESIS | CARBOHYDRATE POLYMERASE | INHIBITORS | CHEMISTRY, MULTIDISCIPLINARY | CHEMICAL SYNTHESIS | Glycosyltransferases - metabolism | Polyisoprenyl Phosphates - chemistry | Biocatalysis | Glycosyltransferases - chemistry | Substrate Specificity | Molecular Structure | Polyisoprenyl Phosphates - metabolism | Research | Catalysis | Analysis | Glycosyltransferases | Genes | Formations | Assembly | Communication
MYCOBACTERIUM-TUBERCULOSIS | ARABINOGALACTAN | PEPTIDOGLYCAN | LENGTH CONTROL | MECHANISM | N-LINKED GLYCOSYLATION | BIOSYNTHESIS | CARBOHYDRATE POLYMERASE | INHIBITORS | CHEMISTRY, MULTIDISCIPLINARY | CHEMICAL SYNTHESIS | Glycosyltransferases - metabolism | Polyisoprenyl Phosphates - chemistry | Biocatalysis | Glycosyltransferases - chemistry | Substrate Specificity | Molecular Structure | Polyisoprenyl Phosphates - metabolism | Research | Catalysis | Analysis | Glycosyltransferases | Genes | Formations | Assembly | Communication
Journal Article
Molecular Microbiology, ISSN 0950-382X, 2007, Volume 65, Issue 4, pp. 1106 - 1121
Summary In Escherichia coli many enzymes including MurG are directly involved in the synthesis and assembly of peptidoglycan. MurG is an essential...
SHAPE | WALL | FTSZ | SPHERICAL CELLS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PENICILLIN-BINDING PROTEINS | MICROBIOLOGY | 1ST MEMBRANE STEP | Z RING | INHIBITORS | N-ACETYLGLUCOSAMINE TRANSFERASE | Cytoplasm - enzymology | Temperature | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Fluorescence | Escherichia coli Proteins - metabolism | Immunoblotting | Cell Wall - enzymology | Escherichia coli - cytology | N-Acetylglucosaminyltransferases - metabolism | Protein Transport | Bacterial Outer Membrane Proteins - metabolism | Models, Biological | Cell Division | Protein Binding | Bacterial Proteins - metabolism | Transferases - metabolism | Escherichia coli
SHAPE | WALL | FTSZ | SPHERICAL CELLS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PENICILLIN-BINDING PROTEINS | MICROBIOLOGY | 1ST MEMBRANE STEP | Z RING | INHIBITORS | N-ACETYLGLUCOSAMINE TRANSFERASE | Cytoplasm - enzymology | Temperature | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Fluorescence | Escherichia coli Proteins - metabolism | Immunoblotting | Cell Wall - enzymology | Escherichia coli - cytology | N-Acetylglucosaminyltransferases - metabolism | Protein Transport | Bacterial Outer Membrane Proteins - metabolism | Models, Biological | Cell Division | Protein Binding | Bacterial Proteins - metabolism | Transferases - metabolism | Escherichia coli
Journal Article
Journal of the American Chemical Society, ISSN 0002-7863, 06/2012, Volume 134, Issue 22, pp. 9343 - 9351
The peptidoglycan glycosyltransferases (GTs) are essential enzymes that catalyze the polymerization of glycan chains of the bacterial cell wall from lipid II...
ACID | GLYCOSYL TRANSFERASE | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | LIPID-II | PENICILLIN-BINDING PROTEINS | MOENOMYCIN | DERIVATIVES | CHEMISTRY, MULTIDISCIPLINARY | CELL-WALL BIOSYNTHESIS | TRANSGLYCOSYLATION STEP | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Structure-Activity Relationship | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan - pharmacology | Molecular Conformation | Peptidoglycan - chemistry | Analysis | Glycosyltransferases | Peptidoglycans | Chemical bonds | Polymerization | Glycosylation | Chemical properties
ACID | GLYCOSYL TRANSFERASE | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | LIPID-II | PENICILLIN-BINDING PROTEINS | MOENOMYCIN | DERIVATIVES | CHEMISTRY, MULTIDISCIPLINARY | CELL-WALL BIOSYNTHESIS | TRANSGLYCOSYLATION STEP | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Structure-Activity Relationship | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan - pharmacology | Molecular Conformation | Peptidoglycan - chemistry | Analysis | Glycosyltransferases | Peptidoglycans | Chemical bonds | Polymerization | Glycosylation | Chemical properties
Journal Article
ACS Chemical Biology, ISSN 1554-8929, 11/2013, Volume 8, Issue 11, pp. 2442 - 2451
Modern medicine is founded on the discovery of penicillin and subsequent small molecules that inhibit bacterial peptidoglycan (PG) and cell wall synthesis....
CELL-WALL SYNTHESIS | METHICILLIN RESISTANCE | TEICHOIC-ACID | BAD BUGS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LIPID-II | BETA-LACTAM ANTIBIOTICS | ANTIBACTERIAL DISCOVERY | BACTERIAL PEPTIDOGLYCAN | Sterols - pharmacology | Staphylococcus aureus - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Sterols - chemistry | Humans | Enzyme Inhibitors - pharmacology | Drug Resistance, Bacterial | Models, Molecular | Pyrazoles - chemistry | Computer Simulation | N-Acetylglucosaminyltransferases - antagonists & inhibitors | Anti-Bacterial Agents - pharmacology | Staphylococcus aureus - drug effects | Bacterial Outer Membrane Proteins - antagonists & inhibitors | Microscopy, Fluorescence | Pyrazoles - pharmacology
CELL-WALL SYNTHESIS | METHICILLIN RESISTANCE | TEICHOIC-ACID | BAD BUGS | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LIPID-II | BETA-LACTAM ANTIBIOTICS | ANTIBACTERIAL DISCOVERY | BACTERIAL PEPTIDOGLYCAN | Sterols - pharmacology | Staphylococcus aureus - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Sterols - chemistry | Humans | Enzyme Inhibitors - pharmacology | Drug Resistance, Bacterial | Models, Molecular | Pyrazoles - chemistry | Computer Simulation | N-Acetylglucosaminyltransferases - antagonists & inhibitors | Anti-Bacterial Agents - pharmacology | Staphylococcus aureus - drug effects | Bacterial Outer Membrane Proteins - antagonists & inhibitors | Microscopy, Fluorescence | Pyrazoles - pharmacology
Journal Article
10.
Full Text
Structural Insight into the Transglycosylation Step of Bacterial Cell-Wall Biosynthesis
Science, ISSN 0036-8075, 3/2007, Volume 315, Issue 5817, pp. 1402 - 1405
Peptidoglycan glycosyltransferases (GTs) catalyze the polymerization step of cell-wall biosynthesis, are membrane-bound, and are highly conserved across all...
Enzymes | Jaw | Antibacterials | Antibiotics | Polymerization | Lipids | Reports | Biochemistry | Diphosphates | Regional identity | Sugars | GLYCOSYLTRANSFERASE MODULE | BACTERIOPHAGE-LAMBDA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | VANCOMYCIN RESISTANCE | PBP1B | STAPHYLOCOCCUS-AUREUS | PROTEINS | KINETIC CHARACTERIZATION | Staphylococcus aureus - enzymology | Molecular Sequence Data | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Oligosaccharides - pharmacology | Penicillin-Binding Proteins - chemistry | Anti-Bacterial Agents - chemistry | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Binding Sites | Staphylococcus aureus - metabolism | Carbohydrate Sequence | Protein Structure, Tertiary | Amino Acid Sequence | Aminoacyltransferases - chemistry | Catalytic Domain | Peptidoglycan Glycosyltransferase - metabolism | Enzyme Inhibitors - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Enzyme Inhibitors - pharmacology | Models, Molecular | Anti-Bacterial Agents - metabolism | Glycosylation | Oligosaccharides - metabolism | Penicillin-Binding Proteins - metabolism | Protein Folding | Amino Acid Motifs | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Cell Wall - metabolism | Apoenzymes - chemistry | Aminoacyltransferases - metabolism | Protein Conformation | Carbohydrate Conformation | Bacterial cell walls | Biosynthesis | Synthesis | Research
Enzymes | Jaw | Antibacterials | Antibiotics | Polymerization | Lipids | Reports | Biochemistry | Diphosphates | Regional identity | Sugars | GLYCOSYLTRANSFERASE MODULE | BACTERIOPHAGE-LAMBDA | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | VANCOMYCIN RESISTANCE | PBP1B | STAPHYLOCOCCUS-AUREUS | PROTEINS | KINETIC CHARACTERIZATION | Staphylococcus aureus - enzymology | Molecular Sequence Data | Multienzyme Complexes - metabolism | Crystallography, X-Ray | Oligosaccharides - pharmacology | Penicillin-Binding Proteins - chemistry | Anti-Bacterial Agents - chemistry | Enzyme Inhibitors - chemistry | Oligosaccharides - chemistry | Binding Sites | Staphylococcus aureus - metabolism | Carbohydrate Sequence | Protein Structure, Tertiary | Amino Acid Sequence | Aminoacyltransferases - chemistry | Catalytic Domain | Peptidoglycan Glycosyltransferase - metabolism | Enzyme Inhibitors - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Enzyme Inhibitors - pharmacology | Models, Molecular | Anti-Bacterial Agents - metabolism | Glycosylation | Oligosaccharides - metabolism | Penicillin-Binding Proteins - metabolism | Protein Folding | Amino Acid Motifs | Multienzyme Complexes - chemistry | Peptidoglycan - biosynthesis | Cell Wall - metabolism | Apoenzymes - chemistry | Aminoacyltransferases - metabolism | Protein Conformation | Carbohydrate Conformation | Bacterial cell walls | Biosynthesis | Synthesis | Research
Journal Article
Biochemical Pharmacology, ISSN 0006-2952, 01/2015, Volume 93, Issue 2, pp. 141 - 150
The glycosyltransferases of family 51 (GT51) catalyze the polymerization of lipid II to form linear glycan chains, which, after cross linking by the...
Moenomycin | Peptidoglycan | Lipid II | SPR | Glycosyltransferase | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | KINETIC CHARACTERIZATION | BINDING PROTEIN 1B | GLYCOSYL TRANSFERASE | LIPID-II | PHARMACOLOGY & PHARMACY | STAPHYLOCOCCUS-AUREUS | TRANSGLYCOSYLATION STEP | Protein Structure, Tertiary | Microbial Interactions - physiology | Bambermycins - metabolism | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Protein Structure, Secondary | Surface Plasmon Resonance - methods | Protein Binding - physiology | Staphylococcus aureus - metabolism
Moenomycin | Peptidoglycan | Lipid II | SPR | Glycosyltransferase | CRYSTAL-STRUCTURE | ESCHERICHIA-COLI | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | KINETIC CHARACTERIZATION | BINDING PROTEIN 1B | GLYCOSYL TRANSFERASE | LIPID-II | PHARMACOLOGY & PHARMACY | STAPHYLOCOCCUS-AUREUS | TRANSGLYCOSYLATION STEP | Protein Structure, Tertiary | Microbial Interactions - physiology | Bambermycins - metabolism | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Protein Structure, Secondary | Surface Plasmon Resonance - methods | Protein Binding - physiology | Staphylococcus aureus - metabolism
Journal Article
Molecular Microbiology, ISSN 0950-382X, 2012, Volume 85, Issue 1, pp. 179 - 194
Growth of the bacterial cell wall peptidoglycan sacculus requires the co-ordinated activities of peptidoglycan synthases, hydrolases and cell morphogenesis...
WALL | PENICILLIN-BINDING-PROTEINS | BACILLUS-SUBTILIS | MREB | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MUREIN | PBP1B | MICROBIOLOGY | GLYCOSYLTRANSFERASE ACTIVITY | MEMBRANE-PROTEINS | DIVISION | Peptidoglycan - biosynthesis | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Cell Wall - metabolism | Escherichia coli Proteins - metabolism | Escherichia coli - growth & development | Penicillin-Binding Proteins - metabolism
WALL | PENICILLIN-BINDING-PROTEINS | BACILLUS-SUBTILIS | MREB | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MUREIN | PBP1B | MICROBIOLOGY | GLYCOSYLTRANSFERASE ACTIVITY | MEMBRANE-PROTEINS | DIVISION | Peptidoglycan - biosynthesis | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Cell Wall - metabolism | Escherichia coli Proteins - metabolism | Escherichia coli - growth & development | Penicillin-Binding Proteins - metabolism
Journal Article
ACS Chemical Biology, ISSN 1554-8929, 12/2013, Volume 8, Issue 12, pp. 2688 - 2696
Understanding the molecular basis of bacterial cell wall assembly is of paramount importance in addressing the threat of increasing antibiotic resistance...
D-AMINO ACIDS | BACTERIAL CELL-WALLS | BACILLUS-MEGATERIUM | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LIPID-II | PENICILLIN-BINDING PROTEINS | GENE DISRUPTION | SYNTHESIZED PEPTIDOGLYCAN | GLYCOSYLTRANSFERASES | Peptidyl Transferases - genetics | Peptidoglycan - chemistry | Uridine Diphosphate N-Acetylmuramic Acid - chemistry | Glutamine - metabolism | Homologous Recombination | Penicillin-Binding Proteins - genetics | Cell Wall - enzymology | Uridine Diphosphate N-Acetylmuramic Acid - metabolism | Cell Wall - drug effects | Penicillin-Binding Proteins - chemistry | Streptococcus pneumoniae - chemistry | Streptococcus pneumoniae - genetics | Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives | Peptidyl Transferases - metabolism | Streptococcus pneumoniae - drug effects | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Peptidyl Transferases - chemistry | Cell Wall - genetics | Peptidoglycan - genetics | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | beta-Lactams - pharmacology | Genetic Engineering | Anti-Bacterial Agents - pharmacology | Glutamic Acid - metabolism | beta-Lactam Resistance - genetics | Streptococcus pneumoniae - enzymology | beta-Lactam Resistance - drug effects | beta-Lactam Resistance | Peptidyl Transferases | Biochemistry, Molecular Biology | Peptidoglycan Glycosyltransferase | beta-Lactams | Streptococcus pneumoniae | Cell Wall | Glutamic Acid | Life Sciences | Penicillin-Binding Proteins | Peptidoglycan | Anti-Bacterial Agents | Uridine Diphosphate N-Acetylmuramic Acid | Biomolecules | Glutamine
D-AMINO ACIDS | BACTERIAL CELL-WALLS | BACILLUS-MEGATERIUM | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | LIPID-II | PENICILLIN-BINDING PROTEINS | GENE DISRUPTION | SYNTHESIZED PEPTIDOGLYCAN | GLYCOSYLTRANSFERASES | Peptidyl Transferases - genetics | Peptidoglycan - chemistry | Uridine Diphosphate N-Acetylmuramic Acid - chemistry | Glutamine - metabolism | Homologous Recombination | Penicillin-Binding Proteins - genetics | Cell Wall - enzymology | Uridine Diphosphate N-Acetylmuramic Acid - metabolism | Cell Wall - drug effects | Penicillin-Binding Proteins - chemistry | Streptococcus pneumoniae - chemistry | Streptococcus pneumoniae - genetics | Uridine Diphosphate N-Acetylmuramic Acid - analogs & derivatives | Peptidyl Transferases - metabolism | Streptococcus pneumoniae - drug effects | Peptidoglycan Glycosyltransferase - metabolism | Peptidoglycan Glycosyltransferase - chemistry | Peptidyl Transferases - chemistry | Cell Wall - genetics | Peptidoglycan - genetics | Cell Wall - chemistry | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Peptidoglycan Glycosyltransferase - genetics | beta-Lactams - pharmacology | Genetic Engineering | Anti-Bacterial Agents - pharmacology | Glutamic Acid - metabolism | beta-Lactam Resistance - genetics | Streptococcus pneumoniae - enzymology | beta-Lactam Resistance - drug effects | beta-Lactam Resistance | Peptidyl Transferases | Biochemistry, Molecular Biology | Peptidoglycan Glycosyltransferase | beta-Lactams | Streptococcus pneumoniae | Cell Wall | Glutamic Acid | Life Sciences | Penicillin-Binding Proteins | Peptidoglycan | Anti-Bacterial Agents | Uridine Diphosphate N-Acetylmuramic Acid | Biomolecules | Glutamine
Journal Article
Chemical Biology & Drug Design, ISSN 1747-0277, 02/2016, Volume 87, Issue 2, pp. 190 - 199
Synthesis of bacterial cell wall peptidoglycan requires glycosyltransferase enzymes that transfer the disaccharide–peptide from lipid II onto the growing...
drug discovery | NMR spectroscopy | glycosyltransferase | penicillin‐binding protein | transglycosylase | penicillin-binding protein | CHEMISTRY, MEDICINAL | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | KINETIC CHARACTERIZATION | ANTIBACTERIAL ACTIVITY | BIOSYNTHESIS | MOENOMYCIN | STAPHYLOCOCCUS-AUREUS | BINDING | Vancomycin - metabolism | Oligosaccharides - pharmacology | Vancomycin - chemistry | Anti-Bacterial Agents - chemistry | Oligosaccharides - chemistry | Vancomycin - pharmacology | Drug Design | Inhibitory Concentration 50 | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Binding Sites | Protein Structure, Tertiary | Bacterial Proteins - antagonists & inhibitors | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Magnetic Resonance Spectroscopy | Anti-Bacterial Agents - metabolism | Oligosaccharides - metabolism | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Cell Wall - metabolism | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Molecular Docking Simulation | Staphylococcus aureus - drug effects | Protein binding
drug discovery | NMR spectroscopy | glycosyltransferase | penicillin‐binding protein | transglycosylase | penicillin-binding protein | CHEMISTRY, MEDICINAL | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | MONOFUNCTIONAL GLYCOSYLTRANSFERASE | KINETIC CHARACTERIZATION | ANTIBACTERIAL ACTIVITY | BIOSYNTHESIS | MOENOMYCIN | STAPHYLOCOCCUS-AUREUS | BINDING | Vancomycin - metabolism | Oligosaccharides - pharmacology | Vancomycin - chemistry | Anti-Bacterial Agents - chemistry | Oligosaccharides - chemistry | Vancomycin - pharmacology | Drug Design | Inhibitory Concentration 50 | Peptidoglycan Glycosyltransferase - antagonists & inhibitors | Penicillin-Binding Proteins - antagonists & inhibitors | Binding Sites | Protein Structure, Tertiary | Bacterial Proteins - antagonists & inhibitors | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Magnetic Resonance Spectroscopy | Anti-Bacterial Agents - metabolism | Oligosaccharides - metabolism | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Cell Wall - metabolism | Bacterial Proteins - metabolism | Anti-Bacterial Agents - pharmacology | Molecular Docking Simulation | Staphylococcus aureus - drug effects | Protein binding
Journal Article
Cell, ISSN 0092-8674, 12/2010, Volume 143, Issue 7, pp. 1110 - 1120
Most bacteria surround themselves with a peptidoglycan (PG) exoskeleton synthesized by polysaccharide polymerases called penicillin-binding proteins (PBPs)....
MORPHOGENESIS | MUTANTS | PEPTIDOGLYCAN BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | COMPLEXES | PENICILLIN-BINDING PROTEINS | PBP1B | HAEMOPHILUS-INFLUENZAE | IDENTIFICATION | DIMERS | CELL BIOLOGY | Peptidoglycan - metabolism | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Escherichia coli Proteins - metabolism | Cell Wall - enzymology | Escherichia coli - cytology | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Bacterial Outer Membrane Proteins - metabolism | Cell Wall - metabolism | Escherichia coli - metabolism | Lipoproteins - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | Polymerization | Enzymes | Polysaccharides | Biosynthesis | Blood lipids | Penicillin | Lipoproteins | Exoskeleton | Antibiotics | Cell walls | Outer membranes | penicillin-binding protein | peptidoglycans | Cofactors
MORPHOGENESIS | MUTANTS | PEPTIDOGLYCAN BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | COMPLEXES | PENICILLIN-BINDING PROTEINS | PBP1B | HAEMOPHILUS-INFLUENZAE | IDENTIFICATION | DIMERS | CELL BIOLOGY | Peptidoglycan - metabolism | Escherichia coli - enzymology | Peptidoglycan Glycosyltransferase - metabolism | Escherichia coli Proteins - metabolism | Cell Wall - enzymology | Escherichia coli - cytology | Penicillin-Binding Proteins - metabolism | Peptidoglycan - biosynthesis | Bacterial Outer Membrane Proteins - metabolism | Cell Wall - metabolism | Escherichia coli - metabolism | Lipoproteins - metabolism | Serine-Type D-Ala-D-Ala Carboxypeptidase - metabolism | Polymerization | Enzymes | Polysaccharides | Biosynthesis | Blood lipids | Penicillin | Lipoproteins | Exoskeleton | Antibiotics | Cell walls | Outer membranes | penicillin-binding protein | peptidoglycans | Cofactors
Journal Article