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Information on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase
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1.14.13.44 2-hydroxybiphenyl 3-monooxygenaseIUBMB Comments
Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl.
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Word Map
- 1.14.13.44
- azelaica
- phenol
- fad
-
2-substituted
- flavin
- 2,3-dihydroxybiphenyl
-
biocatalytic
-
non-substrate
-
laboratory-evolved
-
amberlite
-
fad-dependent
-
entrance
-
ortho-hydroxylation
- flavoprotein
- catechols
- synthesis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
2-hydroxybiphenyl 3-monooxygenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HbpA
oxygenase, 2-hydroxybiphenyl 3-mono-
-
-
-
-
HbpA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
ternary complex mechanism
-
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
ternary complex mechanism
-
-
2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
reduction
-
-
-
-
redox reaction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
,
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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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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
-
-
-
-
?
3-hydroxybiphenyl + NADH + H+ + O2
3,4-dihydroxybiphenyl + NAD+ + H2O
activity of enzyme mutant M321A
-
-
?
2-hydroxybiphenyl + NADH + H+ + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + H+ + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
-
?
2-hydroxybiphenyl + NADH + H+ + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
2-hydroxybiphenyl + NADH + H+ + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
it is suggested that Trp225, which is located in the active site, facilitates proper substrate entrance into the binding pocket
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
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-
-
?
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
-
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
-
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
-
-
-
-
?
2-hydroxybiphenyl + NADH + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
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
-
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol
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-
?
additional information
?
-
-
Asp222 is involved in substrate activation in HbpA
-
-
?
additional information
?
-
-
the substrates partially uncouple oxygen activation from hydroxylation with resultant reduction of both atoms of oxygen to form hydrogen peroxide
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-
?
additional information
?
-
comparisons of substrate binding structures, overview
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additional information
?
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comparisons of substrate binding structures, overview
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additional information
?
-
wild-type enzyme HbpA has a broad substrate range and catalyzes the regioselective ortho-hydroxylation of a wide range of 2-substituted phenols to the corresponding catechols. It possess pro-S enantioselectivity towards the production of several chiral sulfoxides, whereas its mutant variant M321F exhibits improved enantioselectivity, while mutant M321A shows altered regioselectivity by oxidizing 3-hydroxybiphenyl, and thus enabling the production of a distinct antioxidant, 3,4-dihydroxybiphenyl. Identification of substrates and products by GC/MS
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-
-
additional information
?
-
-
Ile244 is located in the substrate binding pocket and is involved in accomodating the phenyl substituent of the phenol
-
-
?
additional information
?
-
-
Asp222 is involved in substrate activation in HbpA
-
-
?
additional information
?
-
-
the substrates partially uncouple oxygen activation from hydroxylation with resultant reduction of both atoms of oxygen to form hydrogen peroxide
-
-
?
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NATURAL SUBSTRATE
NATURAL 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-hydroxybiphenyl + NADH + H+ + O2
2,3-dihydroxybiphenyl + NAD+ + H2O
-
-
-
?
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
-
can replace NADH as electron donor, Km-value for NADPH is much higher than for NADH
FAD
residue Arg242 is suggested to facilitate FAD movement and reduction
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-hydroxymercuribenzoate
-
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
-
0.0031
2-Hydroxybiphenyl
recombinant wild-type enzyme, pH 7.5, 30°C
0.0031
2-Hydroxybiphenyl
pH 7.5, temperature not specified in the publication, mutant enzyme H48A
0.0033
2-Hydroxybiphenyl
pH 7.5, temperature not specified in the publication, wild-type enzyme
0.0048
2-Hydroxybiphenyl
pH 7.5, temperature not specified in the publication R242A
0.005
2-Hydroxybiphenyl
pH 7.5, temperature not specified in the publication, mutant enzyme D117A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numbers for mutant enzymes
-
1.4
2-Hydroxybiphenyl
-
turnover rate refers to the enzyme monomer and not to the tetramer
2.26
2-Hydroxybiphenyl
recombinant wild-type enzyme, pH 7.5, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
729
2-Hydroxybiphenyl
recombinant wild-type enzyme, pH 7.5, 30°C
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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
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2 - 7.8
-
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
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
