EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.44 | 0.0019 | - |
2-Hydroxybiphenyl | - |
Pseudomonas nitroreducens | |
1.14.13.44 | 0.0097 | - |
NADH | reaction with 2-hydroxybiphenyl | Pseudomonas nitroreducens |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.14.13.44 | Pseudomonas nitroreducens | - |
HBP1 | - |
1.14.13.44 | Pseudomonas nitroreducens HBP1 | - |
HBP1 | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.14.13.44 | recombinant enzyme | Pseudomonas nitroreducens |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.14.13.44 | 2-hydroxybiphenyl + NADH + H+ + O2 = 2,3-dihydroxybiphenyl + NAD+ + H2O | ternary complex mechanism | Pseudomonas nitroreducens |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.14.13.44 | 2-hydroxybiphenyl + NADH + O2 | - |
Pseudomonas nitroreducens | 2,3-dihydroxybiphenyl + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-hydroxybiphenyl + NADH + O2 | ternary complex mechanism in which the aromatic substrate has strict control in both the reductive and oxidative half-reaction in a way that reactions leading to substrate hydroxylation are favored over those leading to the futile formation of hydrogen peroxide. NAD+ release from the reduced enzyme-substrate complex is the slowest step in catalysis | Pseudomonas nitroreducens | 2,3-dihydroxybiphenyl + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-hydroxybiphenyl + NADH + O2 | - |
Pseudomonas nitroreducens HBP1 | 2,3-dihydroxybiphenyl + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-hydroxybiphenyl + NADH + O2 | ternary complex mechanism in which the aromatic substrate has strict control in both the reductive and oxidative half-reaction in a way that reactions leading to substrate hydroxylation are favored over those leading to the futile formation of hydrogen peroxide. NAD+ release from the reduced enzyme-substrate complex is the slowest step in catalysis | Pseudomonas nitroreducens HBP1 | 2,3-dihydroxybiphenyl + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-propylphenol + NADH + O2 | - |
Pseudomonas nitroreducens | 1,2-dihydroxy-3-propylbenzene + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-propylphenol + NADH + O2 | - |
Pseudomonas nitroreducens HBP1 | 1,2-dihydroxy-3-propylbenzene + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-sec-butylphenol + NADH + O2 | - |
Pseudomonas nitroreducens | 2-sec-butylcatechol + NAD+ + H2O | - |
? | |
1.14.13.44 | 2-sec-butylphenol + NADH + O2 | - |
Pseudomonas nitroreducens HBP1 | 2-sec-butylcatechol + NAD+ + H2O | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.14.13.44 | 1.4 | - |
2-Hydroxybiphenyl | turnover rate refers to the enzyme monomer and not to the tetramer | Pseudomonas nitroreducens |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.14.13.44 | FAD | flavoenzyme | Pseudomonas nitroreducens | |
1.14.13.44 | NADH | - |
Pseudomonas nitroreducens |