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Literature summary extracted from

  • Cafaro, V.; Izzo, V.; Scognamiglio, R.; Notomista, E.; Capasso, P.; Casbarra, A.; Pucci, P.; Di Donato, A.
    Phenol hydroxylase and toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1: interplay between two enzymes (2004), Appl. Environ. Microbiol., 70, 2211-2219.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.7 0.03779
-
 NADH phenol hydrolxylase component P Pseudomonas stutzeri
1.14.13.7 0.61
-
 phenol reconstituted enzyme complex Pseudomonas stutzeri
1.14.13.7 0.9
-
 NADPH phenol hydrolxylase component P Pseudomonas stutzeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.7 phenol + NADH + H+ + O2 Pseudomonas stutzeri coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation catechol + NAD+ + H2O
-
 ?
1.14.13.7 phenol + NADH + H+ + O2 Pseudomonas stutzeri OX1 coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation catechol + NAD+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.7 Pseudomonas stutzeri
-
-
-
1.14.13.7 Pseudomonas stutzeri OX1
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.7 phenol + NADH + H+ + O2
-
 Pseudomonas stutzeri catechol + NAD+ + H2O
-
 ?
1.14.13.7 phenol + NADH + H+ + O2 coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation Pseudomonas stutzeri catechol + NAD+ + H2O
-
 ?
1.14.13.7 phenol + NADH + H+ + O2
-
 Pseudomonas stutzeri OX1 catechol + NAD+ + H2O
-
 ?
1.14.13.7 phenol + NADH + H+ + O2 coupling between phenol hydroxylase and toluene/o-xylene monooxygenase optimizes the use of nonhydroxylated aromatic molecules by the draining effect of phenol hydroxylase on the products of oxidation catalyzed by toluene/o-xylene monooxygenase, thus avoiding phenol accumulation Pseudomonas stutzeri OX1 catechol + NAD+ + H2O
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.7 0.286
-
 phenol reconstituted enzyme complex Pseudomonas stutzeri

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.7 NADH the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used Pseudomonas stutzeri
1.14.13.7 NADPH the phenol hydrolxylase component P reduces several artificial electron acceptors such as horse heart cytochrome c, 2,6-dichlorophenolindophenol, and potassium ferricyanide, with either NADH or NADPH as electron donor. NADH is preferentially used Pseudomonas stutzeri