EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
   1.13.11.47 | more |
active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview |
Paenarthrobacter nitroguajacolicus |
? |
- |
? |
| 1.13.11.47 | more |
N-heteroaromatic substrate binding and kinetics |
Pseudomonas putida |
? |
- |
? |
| 1.13.11.47 | more |
substrate deprotonation under transient-state conditions is not rate-limiting and shows a pKa value of 7.2 for wild-type. A large solvent isotope effect is found, and the pKa value is shifted to 8.3 in D2O |
Paenarthrobacter nitroguajacolicus |
? |
- |
? |
| 1.13.11.47 | more |
N-heteroaromatic substrate binding and kinetics |
Pseudomonas putida 33/1 |
? |
- |
? |
| 1.13.11.47 | more |
active site cavity and its access, and N-heteroaromatic substrate binding and kinetics, HOD follows a compulsory-order ternary-complex mechanism in which the N-heteroaromatic organic substrate binds to the enzyme prior to dioxygen attack, overview |
Paenarthrobacter nitroguajacolicus Rü61a |
? |
- |
? |
| 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 |
- |
? |
