Manganese Peroxidase, Versatile (MnP)
424.25 $
For reserch purpose only
Shipping cost plus VAT not included , delivery in 7-14 business days
Catalog No
USB-P3351-20
Supplier
US Biologicals
Size
200U
Product Overview
Product Properties
Target Gene
Product Overview
| Description | Versatile peroxidase (VP) from Bjerkandera adusta is a structural hybrid between lignin (LiP) and manganese (MnP) peroxidase. This hybrid combines the catalytic properties of the two above peroxidases, being able to oxidize typical LiP and MnP substrates. The catalytic mechanism is that of classical peroxidases, where the substrate oxidation is carried out by a two-electron multistep reaction at the expense of hydrogen peroxide. Elucidation of the structures of intermediates in this process is crucial for understanding the mechanism of substrate oxidation. In this work, the reaction of H(2)O(2) with the enzyme in the absence of substrate has been investigated with electron paramagnetic resonance (EPR) spectroscopy. The results reveal an EPR signal with partially resolved hyperfine structure typical of an organic radical. The yield of this radical is approximately 30%. Progressive microwave power saturation measurements indicate that the radical is weakly coupled to a paramagnetic metal ion, suggesting an amino acid radical in moderate distance from the ferryl heme. A tryptophan radical was identified as a protein-based radical formed during the catalytic mechanism of VP from Bjerkandera adusta through X-band and high-field EPR measurements at 94 GHz, aided by computer simulations for both frequency bands. A close analysis of the theoretical model of the VP from Bjerkandera sp. shows the presence of a tryptophan residue near to the heme prosthetic group, which is solvent-exposed as in the case of LiP and other VPs. The catalytic role of this residue in a long-range electron-transfer pathway is discussed. Source: Bjerkandera adusta Mn(II):H2O2 oxidoreductases/diarylpropane:O2,H2O2 oxidoreductases 100U/ml (substrate: 1uM Mn(II) or 3,4-dimethoxybenzyl alcohol) at pH 4.5 and 25°C |
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Product Properties
| Storage | -20°C |
| Grade | |
| Purity | Enzymes are produced by fermentation of highly selective fungi and are partly purified. |
| Form | Supplied as a lyophilized powder. No stabilizing proteins added. |
| Reactivity Life | 12 months |
| Note | For reserch purpose only |
Target Gene
NA
