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Literature summary extracted from

  • Hiromoto, T.; Fujiwara, S.; Hosokawa, K.; Yamaguchi, H.
    Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site (2006), J. Mol. Biol., 364, 878-896.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.23 DNA and amino acid sequence determination and analysis, sequence comparisons Comamonas testosteroni

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.13.23 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

EC Number Inhibitors Comment Organism Structure
1.14.13.23 4-chloromercuribenzoate
-
 Comamonas testosteroni

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.23 xenon binding structure of xenon atoms, crystal structure, overview Comamonas testosteroni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.23 3-hydroxybenzoate + NADH + O2 Comamonas testosteroni
-
 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?
1.14.13.23 3-hydroxybenzoate + NADH + O2 Comamonas testosteroni KH122-3s
-
 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.23 Comamonas testosteroni Q6SSJ6
-
-
1.14.13.23 Comamonas testosteroni KH122-3s Q6SSJ6
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.23 3-hydroxybenzoate + NADPH + H+ + O2 = 3,4-dihydroxybenzoate + NADP+ + H2O structural variations in the catalytic action, reaction mechanism Comamonas testosteroni
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.23 3-hydroxybenzoate + NADH + O2
-
 Comamonas testosteroni 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?
1.14.13.23 3-hydroxybenzoate + NADH + O2 substrate recognition and substrate-binding site structure and involved residues, overview Comamonas testosteroni 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?
1.14.13.23 3-hydroxybenzoate + NADH + O2
-
 Comamonas testosteroni KH122-3s 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?
1.14.13.23 3-hydroxybenzoate + NADH + O2 substrate recognition and substrate-binding site structure and involved residues, overview Comamonas testosteroni KH122-3s 3,4-dihydroxybenzoate + NAD+ + H2O
-
 ?
1.14.13.23 additional information the enzyme has a large tunnel for substrate and oxygen access to the active site Comamonas testosteroni ?
-
 ?
1.14.13.23 additional information the enzyme has a large tunnel for substrate and oxygen access to the active site Comamonas testosteroni KH122-3s ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.23 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
1.14.13.23 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

EC Number Synonyms Comment Organism
1.14.13.23 3-hydroxybenzoate hydroxylase
-
 Comamonas testosteroni
1.14.13.23 MHBH
-
 Comamonas testosteroni

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.23 FAD binding site structure Comamonas testosteroni
1.14.13.23 NADPH
-
 Comamonas testosteroni