Application | Comment | Organism |
---|---|---|
drug development | the essential function of the enzyme makes it an attractive antimicrobial target | Staphylococcus aureus |
drug development | the essential function of the enzyme makes it an attractive antimicrobial target | Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide | an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus | Bacillus subtilis | |
2-(3-(2-carbamimidoylhydrazono)-2-oxoindolin-1-yl)-N-(3-nitrophenyl)acetamide | an isatin derivative, active against Gram-positive Bacillus subtilis and Staphylococcus aureus | 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 | Bacillus subtilis | |
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 | Staphylococcus aureus | |
Moenomycin | re-docking of the inhibitor | Bacillus subtilis | |
Moenomycin | re-docking of the inhibitor | Staphylococcus aureus | |
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 | Bacillus subtilis | |
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 | Staphylococcus aureus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
gene PBP2 | - |
Staphylococcus aureus | - |
gene PBP2 | - |
Staphylococcus aureus ATCC 29213 | - |
gene PBP2 | - |
Synonyms | Comment | Organism |
---|---|---|
PBP2 | - |
Staphylococcus aureus |
PBP2 | - |
Bacillus subtilis |
penicillin-binding protein 2 | - |
Staphylococcus aureus |
penicillin-binding protein 2 | - |
Bacillus subtilis |
General Information | Comment | Organism |
---|---|---|
physiological function | 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 | Staphylococcus aureus |
physiological function | 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 | Bacillus subtilis |