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Literature summary for 1.14.13.166 extracted from

  • Kallubai, M.; Amineni, U.; Mallavarapu, M.; Kadiyala, V.
    In silico approach to support that p-nitrophenol monooxygenase from Arthrobacter sp. strain JS443 catalyzes the initial two sequential monooxygenations (2015), Interdiscip. Sci. Comput. Life Sci., 7, 157-167 .
    View publication on PubMed
Search for more literature for 1.14.13.166

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 Comment 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 Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
4-nitrocatechol + NADH + H+ + O2
-
 Lysinibacillus sphaericus 2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
 ?
4-nitrocatechol + NADH + H+ + O2
-
 Arthrobacter sp. JS443 2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
 ?
4-nitrocatechol + NADH + H+ + O2
-
 Lysinibacillus sphaericus JS905 2-hydroxy-1,4-benzoquinone + nitrite + NAD+ + H2O
-
 ?

Synonyms

Synonyms Comment 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 Comment Organism Structure
FAD
-
 Lysinibacillus sphaericus
FAD
-
 Arthrobacter sp. JS443
NADH
-
 Lysinibacillus sphaericus
NADH
-
 Arthrobacter sp. JS443

General Information

General Information Comment 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