Crystallization (Comment) | Organism |
---|---|
structures of the oxygenase subunit CntA. CntA exists in a head-to-tail alpha3 trimeric structure. The Rieske and the catalytic mononuclear iron domains are located more than 40 A apart in the same monomer but adjacent in two neighboring monomers. Tyrosine residue Y203 is essential for ligand recognition through a pi-cation interaction with the quaternary ammonium group | Acinetobacter baumannii |
Protein Variants | Comment | Organism |
---|---|---|
Y203F | mutant is active | Acinetobacter baumannii |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine | - |
Acinetobacter baumannii | |
N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine | - |
Acinetobacter baumannii | |
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide | - |
Acinetobacter baumannii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | the mononuclear Fe exists in an octahedral geometry and is coordinated by two histidine ligands (His213, His208) and a bidentate aspartate residue (Asp 323) in a His-His-Asp catalytic triad | Acinetobacter baumannii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acinetobacter baumannii | A0A059ZPP5 | oxygenase subunit CntA | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-butyl-trimethylammonium + NADH + H+ + O2 | - |
Acinetobacter baumannii | ? + trimethylamine + NAD+ + H2O | - |
? | |
gamma-butyrobetaine + NADH + H+ + O2 | - |
Acinetobacter baumannii | ? + trimethylamine + NAD+ + H2O | - |
? | |
L-carnitine + NADH + H+ + O2 | - |
Acinetobacter baumannii | (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O | - |
? | |
meldonium + NADH + H+ + O2 | - |
Acinetobacter baumannii | ? + trimethylamine + NAD+ + H2O | - |
? | |
additional information | substrates with longer alkyl chains, e.g. hexyl, or other functional groups show no activity | Acinetobacter baumannii | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
CntA | - |
Acinetobacter baumannii |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0011 | - |
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide | pH 7.6, temperature not specified in the publication | Acinetobacter baumannii |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.0011 | - |
pH 7.6, temperature not specified in the publication | Acinetobacter baumannii | 6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine | |
0.0049 | - |
pH 7.6, temperature not specified in the publication | Acinetobacter baumannii | N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide | |
0.0058 | - |
pH 7.6, temperature not specified in the publication | Acinetobacter baumannii | N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine |