6.3.4.14: biotin carboxylase
This is an abbreviated version!
For detailed information about biotin carboxylase, go to the full flat file.
Word Map on EC 6.3.4.14
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6.3.4.14
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carboxyltransferase
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carboxylases
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biotin-dependent
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malonyl-coa
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acetyl-coenzyme
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propionyl-coa
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carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
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carboxyphosphate
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transcarboxylase
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mgatp-dependent
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accases
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atp-grasp
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medicine
- 6.3.4.14
- carboxyltransferase
- carboxylases
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biotin-dependent
- malonyl-coa
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acetyl-coenzyme
- propionyl-coa
- carboxybiotin
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6.4.1.2
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biotin-carboxyl
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biotin-containing
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bicarbonate-dependent
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biotin-binding
- carboxyphosphate
- transcarboxylase
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mgatp-dependent
- accases
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atp-grasp
- medicine
Reaction
Synonyms
ACC, AccA, AccBC, AccC, BC, biotin carboxylase, biotin carboxylase (component of acetyl CoA carboxylase), biotinoyl domain of acetyl-CoA carboxylase, BirA, Carboxylase, biotin, More, PC-beta
ECTree
6.3.4.14 biotin carboxylaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 6.3.4.14 - biotin carboxylase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
6-(2,6-dimethoxyphenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
adenosine diphosphopyridoxal
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ATP, ADP, inorganic phosphate and bicarbonate protect against inhibition
Phosphonoacetate
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competitive inhibition versus ATP, noncompetitive versus bicarbonate
phosphonoacetate linked to the 1'-nitrogen of biotin
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reaction intermediate analog, modest inhibition, competitive versus ATP, noncompetitive versus biotin
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
minimal inhibitory concentration above 64 microg per ml for wild-type, 16 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
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minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N,N-dibenzyl-1,3-oxazole-5-carboxamide
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minimal inhibitory concentration 8 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
minimal inhibitory concentration above 64 microg per ml for wild-type, 8 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
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minimal inhibitory concentration above 64 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
2-amino-N-(2,3-dihydro-1,4-benzodioxin-6-ylmethyl)-N-(2-methylbenzyl)-1,3-oxazole-5-carboxamide
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minimal inhibitory concentration 16 microg per ml for wild-type, 4 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
minimal inhibitory concentration 16 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump tolC and imp gene disruption
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
targets the ATP-binding site of biotin carboxylase. Biophysics of binding, crystallization data. Effective in vivo and in vitro, selective for bacterial biotin carboxylase. Pharmacological studies in rat and mouse
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
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minimal inhibitory concentration 0.125 microg per ml for wild-type, 0.125 microg per ml for mutant with targeted knock-out of efflux pump acrA
6-(2,6-dibromophenyl)pyrido[2,3-d]pyrimidine-2,7-diamine
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minimal inhibitory concentration 1 microg per ml for wild-type, 0.5 microg per ml for mutant with targeted knock-out of efflux pump acrA
ATP
ATP shows substrate inhibition which is competitive against bicarbonate
soraphen A
macrocyclic polyketide natural product, binds to the binding site of phosphorylated Ser222, implying that its inhibition mechanism is the same as that of phosphorylation by AMP-activated protein kinase
soraphen A
nanomolar inhibitor against biotin carboxylase domain of acetyl-coenzyme A carboxylase. The inhibitor may bind in the biotin carboxylase dimer interface and inhibits the biotin carboxylase activity by disrupting the oligomerization of the domain
additional information
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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
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additional information
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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
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additional information
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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
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