Pyridine as novel substrate for regioselective oxygenation with aromatic peroxygenase from Agrocybe aegerita.
FEBS Lett
; 582(29): 4100-6, 2008 Dec 10.
Article
en En
| MEDLINE
| ID: mdl-19022254
ABSTRACT
Agrocybe aegerita peroxidase (AaP) is a versatile extracellular biocatalyst that can oxygenate aromatic compounds. Here, we report on the selective oxidation of pyridine (PY) yielding pyridine N-oxide as sole product. Using H(2)(18)O(2) as co-substrate, the origin of oxygen was confirmed to be the peroxide. Therefore, AaP can be regarded as a true peroxygenase transferring one oxygen atom from peroxide to the substrate. To our best knowledge, there are only two types of enzymes oxidizing PY at the nitrogen bacterial methane monooxygenase and a few P450 monooxygenases. AaP is the first extracellular enzyme and the first peroxidase that catalyzes this reaction, and it converted also substituted PYs into the corresponding N-oxides.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oxígeno
/
Piridinas
/
Agrocybe
/
Hidrocarburos Aromáticos
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Oxigenasas de Función Mixta
Idioma:
En
Revista:
FEBS Lett
Año:
2008
Tipo del documento:
Article
País de afiliación:
Alemania