BRENDA - Enzyme Database
show all sequences of 1.14.13.166

In silico approach to support that p-nitrophenol monooxygenase from Arthrobacter sp. strain JS443 catalyzes the initial two sequential monooxygenations

Kallubai, M.; Amineni, U.; Mallavarapu, M.; Kadiyala, V.; Interdiscip. Sci. Comput. Life Sci. 7, 157-167 (2015)

Data extracted from this reference:

Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-nitrocatechol + NAD(P)H + H+ + O2
Lysinibacillus sphaericus
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
Arthrobacter sp. JS443
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
Lysinibacillus sphaericus JS905
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Arthrobacter sp. JS443
A7YVV2
-
-
Lysinibacillus sphaericus
Q6F4M8 AND Q6F4M9
genes npcA and npcB
-
Lysinibacillus sphaericus JS905
Q6F4M8 AND Q6F4M9
genes npcA and npcB
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Lysinibacillus sphaericus
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Arthrobacter sp. JS443
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Lysinibacillus sphaericus JS905
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Lysinibacillus sphaericus
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Arthrobacter sp. JS443
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Lysinibacillus sphaericus JS905
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
UniProt
Lysinibacillus sphaericus
4-nitrophenol 4-monooxygenase/4-nitrocatechol 2-monooxygenase
UniProt
Arthrobacter sp. JS443
NpcA
-
Lysinibacillus sphaericus
npcB
-
Lysinibacillus sphaericus
PNP monooxygenase
-
Lysinibacillus sphaericus
PNP monooxygenase
-
Arthrobacter sp. JS443
two-component PNP monooxygenase
-
Lysinibacillus sphaericus
two-component PNP monooxygenase
-
Arthrobacter sp. JS443
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
-
Lysinibacillus sphaericus
FAD
-
Arthrobacter sp. JS443
NADH
-
Lysinibacillus sphaericus
NADH
-
Arthrobacter sp. JS443
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
-
Lysinibacillus sphaericus
FAD
-
Arthrobacter sp. JS443
NADH
-
Lysinibacillus sphaericus
NADH
-
Arthrobacter sp. JS443
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-nitrocatechol + NAD(P)H + H+ + O2
Lysinibacillus sphaericus
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
Arthrobacter sp. JS443
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
Lysinibacillus sphaericus JS905
-
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Lysinibacillus sphaericus
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Arthrobacter sp. JS443
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NAD(P)H + H+ + O2
-
745126
Lysinibacillus sphaericus JS905
2-hydroxy-1,4-benzoquinone + nitrite + NAD(P)+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Lysinibacillus sphaericus
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Arthrobacter sp. JS443
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
4-nitrocatechol + NADH + H+ + O2
-
745126
Lysinibacillus sphaericus JS905
2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
-
-
?
General Information
General Information
Commentary
Organism
evolution
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
Lysinibacillus sphaericus
metabolism
the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
Lysinibacillus sphaericus
metabolism
the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
Arthrobacter sp. JS443
additional information
enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. Docking of substrates into the active site of PNP monooxygenase, Arg100, Gln158 and Thr193 are the key catalytic residues, overview
Lysinibacillus sphaericus
additional information
enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. of substrates into the active site of PNP monooxygenase, overview
Arthrobacter sp. JS443
physiological function
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
Lysinibacillus sphaericus
physiological function
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
Arthrobacter sp. JS443
General Information (protein specific)
General Information
Commentary
Organism
evolution
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family
Lysinibacillus sphaericus
metabolism
the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
Lysinibacillus sphaericus
metabolism
the enzyme PNP monoxygenase is involved in the degradation of 4-nitrophenol, proposed pathway, overview. 4-Nitrophenol is converted to 4-nitrocatechol by a 4-nitrophenol 2-monooxygenase, EC 1.14.13.29, of the enzyme, which is subsequently converted to 2-hydroxy-1,4-benzoquinone, EC 1.14.13.166
Arthrobacter sp. JS443
additional information
enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. Docking of substrates into the active site of PNP monooxygenase, Arg100, Gln158 and Thr193 are the key catalytic residues, overview
Lysinibacillus sphaericus
additional information
enzyme structure homology model for PNP monooxygenase using crystal structure of chlorophenol 4-monooxygenase from Burkholderia cepacia AC1100, PDB IS 3HWC, as template. Molecular dynamics simulations performed for docking complexes show the stable interaction between enzyme and substrate 4-nitrocatechol. of substrates into the active site of PNP monooxygenase, overview
Arthrobacter sp. JS443
physiological function
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
Lysinibacillus sphaericus
physiological function
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert 4-nitrophenol to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166
Arthrobacter sp. JS443
Other publictions for EC 1.14.13.166
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)
744109
Min
A two-component para-nitrophe ...
no activity in Rhodococcus imtechensis
Appl. Environ. Microbiol.
82
714-723
2016
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745126
Kallubai
In silico approach to support ...
Arthrobacter sp. JS443, Lysinibacillus sphaericus, Lysinibacillus sphaericus JS905
Interdiscip. Sci. Comput. Life Sci.
7
157-167
2015
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7
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719179
Zhang
Identification of the para-nit ...
Pseudomonas sp., Pseudomonas sp. 1-7
BMC Microbiol.
12
27
2012
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2
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711336
Wei
para-Nitrophenol 4-monooxygena ...
Pseudomonas sp.
Biodegradation
21
915-921
2010
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1
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3
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1
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1
1
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1
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1
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704288
Zhang
Identification and characteriz ...
Pseudomonas sp.
J. Bacteriol.
191
2703-2710
2009
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1
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1
1
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6
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1
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1
1
3
1
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3
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3
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1
3
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3
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718490
Liu
Expression, purification, crys ...
Pseudomonas putida, Pseudomonas putida DLL-E4
Acta Crystallogr. Sect. F
65
1004-1006
2009
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1
1
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1
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5
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1
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2
1
3
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1
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1
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719711
Perry
Cloning of a gene cluster invo ...
Arthrobacter sp.
J. Bacteriol.
189
7563-7572
2007
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1
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5
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1
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15
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2
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1
2
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15
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438817
Leung
The role of the Sphingomonas s ...
Sphingomonas sp., Sphingomonas sp. UG30
FEMS Microbiol. Lett.
173
247-253
1999
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438885
Kadiyala
A two-component monooxygenase ...
Lysinibacillus sphaericus, Lysinibacillus sphaericus JS905
Appl. Environ. Microbiol.
64
2479-2484
1998
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3
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1
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3
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4
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1
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4
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