Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, sequence comparisons | Comamonas testosteroni |
Crystallization (Comment) | Organism |
---|---|
purified native enzyme in complex with substrate 3-hydroxybenzoate or inhibitor 4-chloromercuribenzoate, and as Xe-derivative, sitting drop vapour diffusion method, 10 mg/ml in 25 mM phosphate buffer, pH 7.5, containing 0.3 mM 3-hydroxybenzoate, mixed with an equal volume of a reservoir solution consisting of 0.1 M MES, pH 6.5, 1.3 M ammonium sulfate, and 6% v/v 1,4-dioxane, 20°C, X-ray diffraction structure determination and analysis at 1.8 A and 2.5 A resolution, respectively | Comamonas testosteroni |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
4-chloromercuribenzoate | - |
Comamonas testosteroni |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
xenon | binding structure of xenon atoms, crystal structure, overview | Comamonas testosteroni |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxybenzoate + NADH + O2 | Comamonas testosteroni | - |
3,4-dihydroxybenzoate + NAD+ + H2O | - |
? | |
3-hydroxybenzoate + NADH + O2 | Comamonas testosteroni KH122-3s | - |
3,4-dihydroxybenzoate + NAD+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas testosteroni | Q6SSJ6 | - |
- |
Comamonas testosteroni KH122-3s | Q6SSJ6 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O | structural variations in the catalytic action, reaction mechanism | Comamonas testosteroni |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3-hydroxybenzoate + NADH + O2 | - |
Comamonas testosteroni | 3,4-dihydroxybenzoate + NAD+ + H2O | - |
? | |
3-hydroxybenzoate + NADH + O2 | substrate recognition and substrate-binding site structure and involved residues, overview | Comamonas testosteroni | 3,4-dihydroxybenzoate + NAD+ + H2O | - |
? | |
3-hydroxybenzoate + NADH + O2 | - |
Comamonas testosteroni KH122-3s | 3,4-dihydroxybenzoate + NAD+ + H2O | - |
? | |
3-hydroxybenzoate + NADH + O2 | substrate recognition and substrate-binding site structure and involved residues, overview | Comamonas testosteroni KH122-3s | 3,4-dihydroxybenzoate + NAD+ + H2O | - |
? | |
additional information | the enzyme has a large tunnel for substrate and oxygen access to the active site | Comamonas testosteroni | ? | - |
? | |
additional information | the enzyme has a large tunnel for substrate and oxygen access to the active site | Comamonas testosteroni KH122-3s | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the enzyme forms an active homodimer with crystallographic 2-fold symmetry, in which each subunit consists of the first two domains comprising an active site and the C-terminal domain involved in oligomerization | Comamonas testosteroni |
More | the enzyme has a large tunnel, connecting the substrate binding pocket to the protein surface, for substrate and oxygen access to the active site, fold of the catalytic domain and the active-site architecture, including the FAD and substrate-binding sites, overview | Comamonas testosteroni |
Synonyms | Comment | Organism |
---|---|---|
3-hydroxybenzoate hydroxylase | - |
Comamonas testosteroni |
MHBH | - |
Comamonas testosteroni |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | binding site structure | Comamonas testosteroni | |
NADPH | - |
Comamonas testosteroni |