EC Number   |
General Information  |
Reference |
|---|
   1.14.13.29 | evolution |
PNP monooxygenase belongs to a two-component flavin-diffusible monooxygenase family |
-, 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 |
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 | 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 |
| 1.14.13.29 | metabolism |
PnpA1 is a member of the group D flavin-dependent monooxygenases with an acyl-CoA dehydrogenase fold. Residues Arg100 and His293 are directly involved in catalysis. The bulky side chain of Val292 pushes the substrate toward FAD, hence positioning the substrate properly |
-, 763974 |
| 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 | more |
PnpA1 is the oxygenase component of the two-component PNP 2-monooxygenase from Gram-positive Rhodococcus imtechensis strain RKJ300. It also catalyzes the hydroxylation of 4-nitrocatechol (4NC) and 2-chloro-4-nitrophenol (2C4NP). The crystal structure and site-directed mutagenesis underlined the direct involvement of residues Arg100 and His293 in catalysis. The bulky side chain of residue Val292 is proposed to push the substrate toward flavin adenine dinucleotide (FAD), hence positioning the substrate properly. Different PNP binding manners determine the choice of ortho- or para-hydroxylation on PNP by single-component PNP 4-monooxygenases and two-component PNP 2-monooxygenases. Substrate binding site structure of PnpA1, overview. For two-component flavin-dependent monooxygenases, reduced flavin must be bound to the enzyme before the substrate's entry. The PnpA1-FAD model shows that a substrate can only enter the binding pocket through a narrow hydrophobic tunnel, mainly consisting of Val156, Leu456, and Leu207, because of the prepositioned FAD. The perimeter of the substrate-binding site is mainly made with four fragments including a7, loop 449-454, loop 93-102, and loop 154-175. Among those fragments, loop 449-454 has a relatively high temperature factor and shows the most heterogeneous conformations among the four subunits, reflecting its flexibility. The residues lining the substrate-binding pocket are predominantly hydrophobic ones, including Phe446, Phe155, Phe289, Val292, and Leu207. Molecular docking of FAD and substrates |
763974 |
