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]
Enzymatic reaction of: 2-nitrophenol 2-monooxygenase
EC Number: 18.104.22.1682-nitrophenol + 2 NADPH + oxygen + 2 H+ → catechol + nitrite + 2 NADP+ + H2O
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.
The reaction is physiologically favored in the direction shown.
In Pathways: 2-nitrophenol degradationActivators (Allosteric): Mg2+ [Zeyer88], Mn2+ [Zeyer88] Inhibitors (Competitive): 2,4-dinitrophenol [Zeyer88]Kinetic Parameters:
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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