Information on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.44
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RECOMMENDED NAME
GeneOntology No.
2-hydroxybiphenyl 3-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,2'-dihydroxybiphenyl degradation
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2-hydroxybiphenyl degradation
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
118251-39-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
JM101
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Manually annotated by BRENDA team
JM101
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,2'-dihydroxybiphenyl + NADH + O2
2,2',3-trihydroxybiphenyl + NAD+ + H2O
show the reaction diagram
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-
-
-
?
2,2'-dihydroxybiphenyl + NADPH + O2
2,2',3-trihydroxybiphenyl + NADP+ + H2O
show the reaction diagram
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-
-
-
?
2,5-dihydroxybiphenyl + NADH + O2
2,3,5-trihydroxybiphenyl + NAD+ + H2O
show the reaction diagram
-
-
-
-
?
2-ethylphenol + NADH + O2
1,2-dihydroxy-3-ethylbenzene + NAD+ + H2O
show the reaction diagram
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-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
show the reaction diagram
2-hydroxybiphenyl + NADPH + O2
2,3-dihydroxybiphenyl + NADP+ + H2O
show the reaction diagram
2-hydroxybiphenyl + O2 + NADH + H+
3-phenylcatechol + NAD+ + H2O
show the reaction diagram
2-methylphenol + NADH + O2
1,2-dihydroxy-3-methylbenzene + NAD+ + H2O
show the reaction diagram
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-
-
-
?
2-propylphenol + NADH + O2
1,2-dihydroxy-3-propylbenzene + NAD+ + H2O
show the reaction diagram
2-sec-butylphenol + NADH + O2
2-sec-butylcatechol + NAD+ + H2O
show the reaction diagram
2-sec-butylphenol + NADPH + O2
2-sec-butylcatechol + NADP+ + H2O
show the reaction diagram
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-
-
-
?
2-tert-butylphenol + NADH + O2
1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
show the reaction diagram
guaiacol + NADH + O2
2,3-dihydroxy-methoxybenzene + NAD+ + H2O
show the reaction diagram
indole + NADH + O2
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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can replace NADH as electron donor, Km-value for NADPH is much higher than for NADH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Dihydroxybiphenyl
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inhibits reaction with 2-hydroxybiphenyl
AgNO3
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0.01 mM, complete inhibition
CuSO4
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0.01 mM, complete inhibition
FeSO4
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0.08 mM, 30% inhibition
HgCl2
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0.01 mM, complete inhibition
NaCl
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10 mM, 36% inhibition. 100 mM, 89% inhibition
p-hydroxymercuribenzoate
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partial protection in presence of 2-hydroxybiphenyl, reversed by excess of dithiothreitol
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0034 - 0.004
2,2'-Dihydroxybiphenyl
0.0019 - 0.0031
2-Hydroxybiphenyl
0.0057
2-sec-Butylphenol
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reaction with NADH or NADPH and O2
0.0097 - 0.0268
NADH
0.0943 - 0.137
NADPH
0.0292
O2
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reaction with 2-hydroxybiphenyl and NADH
additional information
additional information
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Km-values for wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9 - 9.4
2,2'-Dihydroxybiphenyl
1.4 - 15.6
2-Hydroxybiphenyl
10.2 - 15.8
2-sec-Butylphenol
0.95
guaiacol
Pseudomonas nitroreducens
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-
0.005 - 0.09
indole
9.8 - 16.2
NADH
11.2 - 18.8
NADPH
16.2
O2
Pseudomonas nitroreducens
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reaction with 2-hydroxybiphenyl and NADH
additional information
additional information
Pseudomonas nitroreducens
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turnover-numbers for mutant enzymes
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.9
2,3-Dihydroxybiphenyl
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
256000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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
native and recombinant enzyme
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recombinant enzyme
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recombinant HbpA
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I244V
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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
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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
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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
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V368A/L417F
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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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis