Species: Pseudomonas putida B2
2-nitrophenol 2-monooxygenase has been purified from Pseudomonas putida B2, a strain that is able to grow on 2-nitrophenol as the sole source of carbon and nitrogen [Zeyer84]. Experiments with a cell-free system showed that the enzyme is inducible by 2-nitrophenol, that the products were catechol and nitrite, and that NADPH is required. The specific activity in the cell-free system was 15 μmol/min/g protein [Zeyer84].
The enzyme was subsequently purified, and was shown to consist of a single polypeptide chain of 58 (gel filtration) or 65 (SDS-polyacrylamide gel) kDa [Zeyer88]. The enzyme was soluble, and consumed one molecule of molecular oxygen per molecule 2-nitrophenol converted.
Molecular Weight of Polypeptide: 58.0 kD (experimental) [Zeyer88 ]
|Cellular Component:||GO:0005829 - cytosol [Zeyer88]|
Enzymatic reaction of: 2-nitrophenol 2-monooxygenase
EC Number: 18.104.22.168
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
In Pathways: 2-nitrophenol degradation
pH(opt): 7.5-8 [Zeyer88]
Zeyer88: Zeyer J, Kocher HP (1988). "Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite." J Bacteriol 170(4);1789-94. PMID: 3350791
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