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Literature summary for 2.4.1.129 extracted from

  • 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 (2014), Chem. Biol. Drug Des., 84, 685-696.
    View publication on PubMed

Application

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

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

Organism UniProt Comment Textmining
Bacillus subtilis
-
gene PBP2
-
Staphylococcus aureus
-
gene PBP2
-
Staphylococcus aureus ATCC 29213
-
gene PBP2
-

Synonyms

Synonyms Comment Organism
PBP2
-
Staphylococcus aureus
PBP2
-
Bacillus subtilis
penicillin-binding protein 2
-
Staphylococcus aureus
penicillin-binding protein 2
-
Bacillus subtilis

General Information

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