EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinaldine + O2 |
- |
Arthrobacter sp. |
N-Acetylanthranilate + CO |
- |
? |
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinaldine + O2 |
- |
Arthrobacter sp. Ru61a |
N-Acetylanthranilate + CO |
- |
? |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 |
- |
Paenarthrobacter nitroguajacolicus |
N-acetylanthranilic acid + CO |
- |
? |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 |
HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism |
Paenarthrobacter nitroguajacolicus |
N-acetylanthranilic acid + CO |
- |
? |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 |
- |
Paenarthrobacter nitroguajacolicus Rü61a |
N-acetylanthranilic acid + CO |
- |
? |
1.13.11.47 | 1H-3-hydroxy-4-oxoquinaldine + O2 |
HOD possesses a classical alpha/beta-hydrolase fold core domain additionally equipped with a cap domain. Organic substrates bind in a preorganized active site with an orientation ideally suited for selective deprotonation of their hydroxyl group by a His/Asp charge-relay system affording the generation of electron-donating species. The oxyanion hole of the alpha/beta-hydrolase fold, typically employed to stabilize the tetrahedral intermediate in ester hydrolysis reactions, is utilized here to host and control oxygen chemistry, which is proposed to involve a peroxide anion intermediate. Product release by proton back transfer from the catalytic histidine is driven by minimization of intramolecular charge repulsion. Structural and kinetic data suggest a nonnucleophilic general-base mechanism |
Paenarthrobacter nitroguajacolicus Rü61a |
N-acetylanthranilic acid + CO |
- |
? |
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinoline + O2 |
- |
Pseudomonas putida |
N-Formylanthranilate + CO |
- |
? |
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinoline + O2 |
at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine |
Arthrobacter sp. |
N-Formylanthranilate + CO |
- |
? |
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinoline + O2 |
- |
Pseudomonas putida 33/1 |
N-Formylanthranilate + CO |
- |
? |
1.13.11.47 | 1H-3-Hydroxy-4-oxoquinoline + O2 |
at 20% of the activity with 1H-3-Hydroxy-4-oxoquinaldine |
Arthrobacter sp. Ru61a |
N-Formylanthranilate + CO |
- |
? |