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Enzyme Nomenclature
Information on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase
Word Map on EC 1.14.13.44
- 1.14.13.44
- azelaica
- phenol
- 2,3-dihydroxybiphenyl
-
biocatalytic
-
flavoprotein
-
fad-dependent
- fad
-
amberlite
-
non-substrate
- catechols
- flavin
-
laboratory-evolved
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2-substituted
-
resin
-
ortho-hydroxylation
- methanol
- synthesis
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.14.13.44
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RECOMMENDED NAME
GeneOntology No.
2-hydroxybiphenyl 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
ternary complex mechanism
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2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
ternary complex mechanism
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2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
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redox reaction
reduction
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-
-
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redox reaction
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
2-hydroxybiphenyl,NADH:oxygen oxidoreductase (3-hydroxylating)
Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl.
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CAS REGISTRY NUMBER
COMMENTARY
118251-39-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,2'-dihydroxybiphenyl + NADH + O2
2,2',3-trihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2,2'-dihydroxybiphenyl + NADPH + O2
2,2',3-trihydroxybiphenyl + NADP+ + H2O
-
-
-
-
?
2,5-dihydroxybiphenyl + NADH + O2
2,3,5-trihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2-ethylphenol + NADH + O2
1,2-dihydroxy-3-ethylbenzene + NAD+ + H2O
-
-
-
-
?
2-methylphenol + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O
-
-
-
-
?
2-sec-butylphenol + NADPH + O2
2-sec-butylcatechol + NADP+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
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
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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the activity of the mutant enzyme HbpAind is six times lower than that of the wild-type enzyme
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-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
first enzyme of 2-hydroxybiphenyl degradation
-
-
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2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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first enzyme of the 2-hydroxybiphenyl degradation pathway
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-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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the activity of the mutant enzyme HbpAind is six times lower than that of the wild-type enzyme
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
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
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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first enzyme of 2-hydroxybiphenyl degradation
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-
-
2-hydroxybiphenyl + NADPH + O2
2,3-dihydroxybiphenyl + NADP+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADPH + O2
2,3-dihydroxybiphenyl + NADP+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + O2 + NADH + H+
3-phenylcatechol + NAD+ + H2O
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-
-
-
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2-propylphenol + NADH + O2
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
-
?
2-propylphenol + NADH + O2
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
-
-
-
-
?
2-sec-butylphenol + NADH + O2
2-sec-butylcatechol + NAD+ + H2O
-
-
-
-
?
2-sec-butylphenol + NADH + O2
2-sec-butylcatechol + NAD+ + H2O
-
-
-
-
?
2-tert-butylphenol + NADH + O2
1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
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-
-
-
?
2-tert-butylphenol + NADH + O2
1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
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-
-
-
?
guaiacol + NADH + O2
2,3-dihydroxy-methoxybenzene + NAD+ + H2O
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i.e. 2-methoxyphenol
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-
?
guaiacol + NADH + O2
2,3-dihydroxy-methoxybenzene + NAD+ + H2O
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i.e. 2-methoxyphenol
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?
additional information
?
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Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol
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-
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additional information
?
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Asp222 is involved in substrate activation in HbpA
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-
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additional information
?
-
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the substrates partially uncouple oxygen activation from hydroxylation with resultant reduction of both atoms of oxygen to form hydrogen peroxide
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-
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additional information
?
-
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Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol
-
-
-
additional information
?
-
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Asp222 is involved in substrate activation in HbpA
-
-
-
additional information
?
-
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the substrates partially uncouple oxygen activation from hydroxylation with resultant reduction of both atoms of oxygen to form hydrogen peroxide
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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
first enzyme of 2-hydroxybiphenyl degradation
-
-
-
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
first enzyme of the 2-hydroxybiphenyl degradation pathway
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
first enzyme of 2-hydroxybiphenyl degradation
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
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can replace NADH as electron donor, Km-value for NADPH is much higher than for NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-hydroxymercuribenzoate
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partial protection in presence of 2-hydroxybiphenyl, reversed by excess of dithiothreitol
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km-values for wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Pseudomonas nitroreducens
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turnover-numbers for mutant enzymes
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1.4
2-Hydroxybiphenyl
Pseudomonas nitroreducens
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turnover rate refers to the enzyme monomer and not to the tetramer
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.8
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more than 80% of maximal activity at pH 7.2 and pH 7.8, beyond pH 7.8 activity declines abruptly with increasing pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
256000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour-diffusion, optimized precipitant solution contains 1.6 M ammonium sulfate, 100 mM sodium chloride and 100 mM MES-NaOH, pH 7.5, crystals of native and SeMet-HbpA diffract to 2.01 and 2.25 A, respectively
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20�C, pure enzyme at concentration of 3.8 mg/ml in 50 mM phosphate buffer, pH 7.5, stable for at least 6 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I244V
-
mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase
V368A/L417F
-
double replacement improves the efficiency of substrate hydroxylation by reducing the uncoupled oxidation of NADH. With guaiacol as substrate, the Vmax is increased and the Km-value is decreased. With 2-tert-butylphenol as substrate the turnover number is increased more than 5fold
I244V
-
mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase
-
V368A/L417F
-
double replacement improves the efficiency of substrate hydroxylation by reducing the uncoupled oxidation of NADH. With guaiacol as substrate, the Vmax is increased and the Km-value is decreased. With 2-tert-butylphenol as substrate the turnover number is increased more than 5fold
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additional information
additional information
-
direct enzyme evolution of EC 1.14.13.44 results in an enzyme variant HbpAind, that hydroxylates indole and indole derivatives such as hydroxyindoles and 5-bromoindole. The wild-type protein does not catalyze theses reactions. HbpAind contains amino acid substitutions D222V and V368A. The activity for indole hydroxylation is increased 18fold in this variant
additional information
-
direct enzyme evolution of EC 1.14.13.44 results in an enzyme variant HbpAind, that hydroxylates indole and indole derivatives such as hydroxyindoles and 5-bromoindole. The wild-type protein does not catalyze theses reactions. HbpAind contains amino acid substitutions D222V and V368A. The activity for indole hydroxylation is increased 18fold in this variant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
-
production of 3-phenylcatechol, which is starting material for the synthesis of pharmaceutical compounds and artificial supramolecular systems
synthesis
-
production of 3-phenylcatechol, which is starting material for the synthesis of pharmaceutical compounds and artificial supramolecular systems
-
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.44)
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