1.14.13.44: 2-hydroxybiphenyl 3-monooxygenase
This is an abbreviated version!
For detailed information about 2-hydroxybiphenyl 3-monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.44
-
1.14.13.44
-
azelaica
-
phenol
-
fad
-
2-substituted
-
flavin
-
2,3-dihydroxybiphenyl
-
ortho-hydroxylation
-
entrance
-
amberlite
-
flavoprotein
-
laboratory-evolved
-
biocatalytic
-
non-substrate
-
fad-dependent
-
catechols
-
synthesis
- 1.14.13.44
- azelaica
- phenol
- fad
-
2-substituted
- flavin
- 2,3-dihydroxybiphenyl
-
ortho-hydroxylation
-
entrance
-
amberlite
- flavoprotein
-
laboratory-evolved
-
biocatalytic
-
non-substrate
-
fad-dependent
- catechols
- synthesis
Reaction
Synonyms
2-hydroxybiphenyl 3-monooxygenase, HbpA, oxygenase, 2-hydroxybiphenyl 3-mono-
ECTree
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12
Substrates Products
Substrates Products on EC 1.14.13.44 - 2-hydroxybiphenyl 3-monooxygenase
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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 + 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
-
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
-
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
-
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
-
-
-
?
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
-
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
-
-
?
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
-
-
-
-
?
2-tert-butylphenol + NADH + O2
1,2-dihydroxy-3-tert-butylbenzene + NAD+ + H2O
-
-
-
-
?
guaiacol + NADH + O2
2,3-dihydroxy-methoxybenzene + NAD+ + H2O
-
i.e. 2-methoxyphenol
-
-
?
guaiacol + NADH + O2
2,3-dihydroxy-methoxybenzene + NAD+ + H2O
-
i.e. 2-methoxyphenol
-
-
?
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
-
-
?
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
-
-
?
