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Literature summary extracted from

  • Brylinski, M.; Waldrop, G.L.
    Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries (2014), Molecules, 19, 4021-4045 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.4.14 in-silico docking studies of amino-oxazole inhibitors Staphylococcus aureus
6.3.4.14 in-silico docking studies of amino-oxazole inhibitors Haemophilus influenzae
6.3.4.14 in-silico docking studies of amino-oxazole inhibitors Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.4.14 additional information docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233 Escherichia coli
6.3.4.14 additional information docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233 Haemophilus influenzae
6.3.4.14 additional information docking studies of amino-oxazole inhibitors to biotin carboxylase from Escherichia coli, Haemophilus influenzae, Pseudomonas aeruginosa, Enterococcus faecalis, Staphylococcus aureus and others. Binding of the amino-oxazole anchor is stabilized by a network of hydrogen bonds to residues 201, 202 and 204. Halogenated aromatic moieties attached to the amino-oxazole scaffold enhance interactions with a hydrophobic pocket formed by residues 157, 169, 171 and 203. Larger substituents reach deeper into the binding pocket to form additional hydrogen bonds with the side chains of residues 209 and 233 Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.14 Escherichia coli
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6.3.4.14 Haemophilus influenzae
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6.3.4.14 Staphylococcus aureus
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