BRENDA - Enzyme Database
show all sequences of 1.14.13.44

Catalytic mechanism of 2-hydroxybiphenyl 3-monooxygenase, a flavoprotein from Pseudomonas azelaica HBP1

Suske, W.A.; Van Berkel, W.J.H.; Kohler, H.P.E.; J. Biol. Chem. 274, 33355-33365 (1999)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0019
-
2-Hydroxybiphenyl
-
Pseudomonas nitroreducens
0.0097
-
NADH
reaction with 2-hydroxybiphenyl
Pseudomonas nitroreducens
Organism
Organism
UniProt
Commentary
Textmining
Pseudomonas nitroreducens
-
HBP1
-
Pseudomonas nitroreducens HBP1
-
HBP1
-
Purification (Commentary)
Purification (Commentary)
Organism
recombinant enzyme
Pseudomonas nitroreducens
Reaction
Reaction
Commentary
Organism
Reaction ID
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
ternary complex mechanism
Pseudomonas nitroreducens
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2-hydroxybiphenyl + NADH + O2
-
438849
Pseudomonas nitroreducens
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens
?
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
438849
Pseudomonas nitroreducens
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens
?
2-hydroxybiphenyl + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens HBP1
?
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
438849
Pseudomonas nitroreducens HBP1
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens HBP1
?
2-propylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
?
2-propylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
?
2-sec-butylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens
2-sec-butylcatechol + NAD+ + H2O
-
-
-
?
2-sec-butylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
2-sec-butylcatechol + NAD+ + H2O
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
2-Hydroxybiphenyl
turnover rate refers to the enzyme monomer and not to the tetramer
Pseudomonas nitroreducens
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavoenzyme
Pseudomonas nitroreducens
NADH
-
Pseudomonas nitroreducens
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavoenzyme
Pseudomonas nitroreducens
NADH
-
Pseudomonas nitroreducens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0019
-
2-Hydroxybiphenyl
-
Pseudomonas nitroreducens
0.0097
-
NADH
reaction with 2-hydroxybiphenyl
Pseudomonas nitroreducens
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant enzyme
Pseudomonas nitroreducens
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2-hydroxybiphenyl + NADH + O2
-
438849
Pseudomonas nitroreducens
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens
?
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
438849
Pseudomonas nitroreducens
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens
?
2-hydroxybiphenyl + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens HBP1
?
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
438849
Pseudomonas nitroreducens HBP1
2,3-dihydroxybiphenyl + NAD+ + H2O
-
438849
Pseudomonas nitroreducens HBP1
?
2-propylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
?
2-propylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
?
2-sec-butylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens
2-sec-butylcatechol + NAD+ + H2O
-
-
-
?
2-sec-butylphenol + NADH + O2
-
438849
Pseudomonas nitroreducens HBP1
2-sec-butylcatechol + NAD+ + H2O
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
1.4
-
2-Hydroxybiphenyl
turnover rate refers to the enzyme monomer and not to the tetramer
Pseudomonas nitroreducens
Other publictions for EC 1.14.13.44
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744407
Kanteev
A crystal structure of 2-hydr ...
Pseudomonas nitroreducens
Biochim. Biophys. Acta
1854
1906-1913
2015
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-
1
1
6
-
-
12
-
-
-
-
-
5
-
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1
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-
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-
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2
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2
-
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12
-
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1
-
-
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1
1
1
6
-
-
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12
-
-
-
-
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-
1
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-
-
-
2
-
-
-
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12
-
-
-
-
-
-
-
-
12
12
744702
Jensen
Structures of the Apo and FAD ...
Pseudomonas nitroreducens
ChemBioChem
16
968-976
2015
-
-
1
1
-
-
-
4
-
-
-
-
-
3
-
-
1
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-
-
-
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1
1
1
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-
-
1
-
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1
-
-
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-
1
1
1
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-
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-
4
-
-
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1
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-
1
1
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-
1
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-
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-
-
-
657455
Meyer
Crystallization and preliminar ...
Pseudomonas nitroreducens
Acta Crystallogr. Sect. D
59
741-743
2003
-
-
1
1
-
-
3
-
-
-
1
1
-
7
-
-
1
-
-
-
-
-
2
1
1
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
1
-
-
-
3
-
-
-
-
1
1
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
438847
Meyer
Changing the substrate reactiv ...
Pseudomonas nitroreducens, Pseudomonas nitroreducens HBP1
J. Biol. Chem.
277
5575-5582
2002
-
-
-
-
2
-
-
1
-
-
-
-
-
10
-
-
-
-
-
-
-
-
10
-
-
-
-
-
4
-
-
-
2
-
-
-
-
-
-
2
-
2
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
438848
Meyer
Hydroxylation of indole by lab ...
Pseudomonas nitroreducens, Pseudomonas nitroreducens HBP1
J. Biol. Chem.
277
34161-34167
2002
-
-
-
-
1
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
6
-
-
-
-
-
4
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
438849
Suske
Catalytic mechanism of 2-hydro ...
Pseudomonas nitroreducens, Pseudomonas nitroreducens HBP1
J. Biol. Chem.
274
33355-33365
1999
-
-
-
-
-
-
-
2
-
-
-
-
-
10
-
-
1
1
-
-
-
-
8
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
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-
-
1
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-
-
-
8
-
-
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-
1
-
-
-
-
-
-
-
-
-
-
658323
Held
An integrated process for the ...
Escherichia coli, Escherichia coli JM101
Biotechnol. Bioeng.
62
641-648
1999
-
1
-
-
-
-
-
-
-
-
-
-
-
12
-
-
-
-
-
-
-
-
2
-
-
1
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-
-
-
-
-
1
-
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1
-
1
-
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-
-
-
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-
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-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
438850
Suske
Purification and characterizat ...
Pseudomonas nitroreducens, Pseudomonas nitroreducens HBP1
J. Biol. Chem.
272
24257-24265
1997
-
-
-
-
-
-
7
10
-
-
2
2
-
16
-
-
1
-
-
-
1
1
18
1
-
-
-
-
11
1
1
-
3
1
-
-
-
-
-
3
-
-
-
-
7
1
10
-
-
2
2
-
-
-
1
-
-
1
1
18
1
-
-
-
11
1
1
-
-
-
-
-
-
-
-