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Literature summary extracted from

  • Suske, W.A.; Van Berkel, W.J.H.; Kohler, H.P.E.
    Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1 (1999), J. Biol. Chem., 274, 33355-33365.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.44 0.0019
-
2-Hydroxybiphenyl
-
Pseudomonas nitroreducens
1.14.13.44 0.0097
-
NADH reaction with 2-hydroxybiphenyl Pseudomonas nitroreducens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.44 Pseudomonas nitroreducens
-
HBP1
-
1.14.13.44 Pseudomonas nitroreducens HBP1
-
HBP1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.44 recombinant enzyme Pseudomonas nitroreducens

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.44 2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O ternary complex mechanism Pseudomonas nitroreducens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.44 2-hydroxybiphenyl + NADH + O2
-
Pseudomonas nitroreducens 2,3-dihydroxybiphenyl + NAD+ + H2O
-
?
1.14.13.44 2-hydroxybiphenyl + NADH + O2 ternary complex mechanism in which the aromatic substrate has strict control in both the reductive and oxidative half-reaction in a way that reactions leading to substrate hydroxylation are favored over those leading to the futile formation of hydrogen peroxide. NAD+ release from the reduced enzyme-substrate complex is the slowest step in catalysis Pseudomonas nitroreducens 2,3-dihydroxybiphenyl + NAD+ + H2O
-
?
1.14.13.44 2-hydroxybiphenyl + NADH + O2
-
Pseudomonas nitroreducens HBP1 2,3-dihydroxybiphenyl + NAD+ + H2O
-
?
1.14.13.44 2-hydroxybiphenyl + NADH + O2 ternary complex mechanism in which the aromatic substrate has strict control in both the reductive and oxidative half-reaction in a way that reactions leading to substrate hydroxylation are favored over those leading to the futile formation of hydrogen peroxide. NAD+ release from the reduced enzyme-substrate complex is the slowest step in catalysis Pseudomonas nitroreducens HBP1 2,3-dihydroxybiphenyl + NAD+ + H2O
-
?
1.14.13.44 2-propylphenol + NADH + O2
-
Pseudomonas nitroreducens 1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
?
1.14.13.44 2-propylphenol + NADH + O2
-
Pseudomonas nitroreducens HBP1 1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
?
1.14.13.44 2-sec-butylphenol + NADH + O2
-
Pseudomonas nitroreducens 2-sec-butylcatechol + NAD+ + H2O
-
?
1.14.13.44 2-sec-butylphenol + NADH + O2
-
Pseudomonas nitroreducens HBP1 2-sec-butylcatechol + NAD+ + H2O
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.44 1.4
-
2-Hydroxybiphenyl turnover rate refers to the enzyme monomer and not to the tetramer Pseudomonas nitroreducens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.44 FAD flavoenzyme Pseudomonas nitroreducens
1.14.13.44 NADH
-
Pseudomonas nitroreducens