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Literature summary for 1.14.13.23 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)

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

Crystallization (Commentary)

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

Inhibitors Comment Organism Structure
4-chloromercuribenzoate
-
Comamonas testosteroni

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Comamonas testosteroni Q6SSJ6
-
-
Comamonas testosteroni KH122-3s Q6SSJ6
-
-

Reaction

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 and Products (Substrate)

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

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

Synonyms Comment Organism
3-hydroxybenzoate hydroxylase
-
Comamonas testosteroni
MHBH
-
Comamonas testosteroni

Cofactor

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