Reaction participants Show >> << Hide
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Namehelp_outline
Fe(III)-[cytochrome c]
Identifier
RHEA-COMP:14399
Reactive part
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- Name help_outline Fe3+ Identifier CHEBI:29034 (CAS: 20074-52-6) help_outline Charge 3 Formula Fe InChIKeyhelp_outline VTLYFUHAOXGGBS-UHFFFAOYSA-N SMILEShelp_outline [Fe+3] 2D coordinates Mol file for the small molecule Search links Involved in 248 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pseudooxynicotine Identifier CHEBI:66878 Charge 1 Formula C10H15N2O InChIKeyhelp_outline SGDIDUFQYHRMPR-UHFFFAOYSA-O SMILEShelp_outline C[NH2+]CCCC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-oxo-4-(pyridin-3-yl)butanal Identifier CHEBI:66879 (CAS: 76014-80-7) help_outline Charge 0 Formula C9H9NO2 InChIKeyhelp_outline CFONOJVUTZAMCB-UHFFFAOYSA-N SMILEShelp_outline O=CCCC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
Fe(II)-[cytochrome c]
Identifier
RHEA-COMP:10350
Reactive part
help_outline
- Name help_outline Fe2+ Identifier CHEBI:29033 (CAS: 15438-31-0) help_outline Charge 2 Formula Fe InChIKeyhelp_outline CWYNVVGOOAEACU-UHFFFAOYSA-N SMILEShelp_outline [Fe++] 2D coordinates Mol file for the small molecule Search links Involved in 263 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline methylamine Identifier CHEBI:59338 Charge 1 Formula CH6N InChIKeyhelp_outline BAVYZALUXZFZLV-UHFFFAOYSA-O SMILEShelp_outline C[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 27 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:75351 | RHEA:75352 | RHEA:75353 | RHEA:75354 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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The enzyme pseudooxynicotine amine oxidase from Pseudomonas putida S16 is not an oxidase, but a dehydrogenase.
Choudhary V., Wu K., Zhang Z., Dulchavsky M., Barkman T., Bardwell J.C.A., Stull F.
The soil-dwelling bacterium Pseudomonas putida S16 can survive on nicotine as its sole carbon and nitrogen source. The enzymes nicotine oxidoreductase (NicA2) and pseudooxynicotine amine oxidase (Pnao), both members of the flavin-containing amine oxidase family, catalyze the first two steps in the ... >> More
The soil-dwelling bacterium Pseudomonas putida S16 can survive on nicotine as its sole carbon and nitrogen source. The enzymes nicotine oxidoreductase (NicA2) and pseudooxynicotine amine oxidase (Pnao), both members of the flavin-containing amine oxidase family, catalyze the first two steps in the nicotine catabolism pathway. Our laboratory has previously shown that, contrary to other members of its enzyme family, NicA2 is actually a dehydrogenase that uses a cytochrome c protein (CycN) as its electron acceptor. The natural electron acceptor for Pnao is unknown; however, within the P. putida S16 genome, pnao forms an operon with cycN and nicA2, leading us to hypothesize that Pnao may also be a dehydrogenase that uses CycN as its electron acceptor. Here we characterized the kinetic properties of Pnao and show that Pnao is poorly oxidized by O<sub>2</sub>, but can be rapidly oxidized by CycN, indicating that Pnao indeed acts as a dehydrogenase that uses CycN as its oxidant. Comparing steady-state kinetics with transient kinetic experiments revealed that product release primarily limits turnover by Pnao. We also resolved the crystal structure of Pnao at 2.60 Å, which shows that Pnao has a similar structural fold as NicA2. Furthermore, rigid-body docking of the structure of CycN with Pnao and NicA2 identified a potential conserved binding site for CycN on these two enzymes. Taken together, our results demonstrate that although Pnao and NicA2 show a high degree of similarity to flavin containing amine oxidases that use dioxygen directly, both enzymes are actually dehydrogenases. << Less