EC Number   |
General Information |
Reference  |
|---|
   1.14.13.29 | metabolism |
NphA1 oxidizes 4-nitrophenol into 4-nitrocatechol in the presence of FAD, NADH and NphA2 (reduces FAD in the presence of NADH) |
698597 |
| 1.14.13.29 | evolution |
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family |
-, 745126 |
| 1.14.13.29 | 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 |
-, 745126 |
| 1.14.13.29 | more |
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 |
745126 |
| 1.14.13.29 | more |
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 |
-, 745126 |
| 1.14.13.29 | 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 |
745126 |
| 1.14.13.29 | physiological function |
the enzyme comprises two components, a flavoprotein reductase and an oxygenase, catalyzes the initial two sequential monooxygenations to convert PNP to trihydroxybenzene, EC 1.14.13.29 and EC 1.14.13.166 |
-, 745126 |
| 1.14.13.29 | evolution |
PnpA1 is structurally determined to be a member of the group D flavin-dependent monooxygenases with an acyl coenzyme A (acyl-CoA) dehydrogenase fold, crystal structure analysis, overview. PnpA1 shows an obvious difference in substrate selectivity with its close homologues TcpA and TftD, which may be caused by the unique Thr296 and a different conformation in the loop from positions 449 to 454 (loop 449-454) |
-, 763974 |
| 1.14.13.29 | malfunction |
an N450A variant is found with improved activity for 4NC and 2C4NP, probably because of reduced steric hindrance |
-, 763974 |
| 1.14.13.29 | metabolism |
para-nitrophenol (PNP) is a hydrolytic product of organophosphate insecticides, such as parathion and methylparathion, in soil. Aerobic microbial degradation of PNP has been classically shown to proceed via the benzenetriol (BT) pathway in Gram-positive degraders. The BT pathway is initiated by a two-component PNP 2-monooxygenase. Comparison of the degradation pathways in Gram-negative and Gram-positive strains. Degradation pathways of PNP and 4NC in Gram-negative strains. PNP and 4NC are oxidized to p-benzoquinone and hydroxyl-1,4-benzoquinone, respectively, and the latter two can be reduced and degraded by other enzymes. Degradation pathways of PNP and 2C4NP in Gram-positive strains. PnpA1 oxidizes PNP to 4NC, and the latter is further oxidized to hydroxyl-1,4-benzoquinone, which can be nonenzymatically reduced to BT. 2C4NP can also be oxidized to produce chloro-1,4-benzoquinone, which is immediately converted to hydroxyl-1,4-benzoquinone by hydrolytic dechlorination and reduced to BT |
-, 763974 |
