Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

The electron in the PrnD Rieske oxygenase can be transferred by either of two pathways, one involving Asp183′ and the other involving Asn180′. Active site modeling of dimerization interface in combination with site-directed mutagenesis indicates that the electron in the PrnD Rieske oxygenase can be...

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Veröffentlicht in:	Bioorganic & medicinal chemistry letters 2011-05, Vol.21 (10), p.2873-2876
Hauptverfasser:	Tiwari, Manish Kumar, Lee, Jung-Kul, Moon, Hee-Jung, Zhao, Huimin
Format:	Artikel
Sprache:	eng
Schlagworte:	Active site modeling active sites Amines - chemistry Aminopyrrolnitrin oxygenase (PrnD) Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences catalytic activity dimerization Electron transfer Electrophoresis, Polyacrylamide Gel Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology gene overexpression Isc operon Models, Molecular Mutagenesis, Site-Directed operon Overexpression Oxidoreductases Oxygenases - chemistry Oxygenases - genetics Pyrrolnitrin - chemistry site-directed mutagenesis
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Beschreibung
Zusammenfassung:	The electron in the PrnD Rieske oxygenase can be transferred by either of two pathways, one involving Asp183′ and the other involving Asn180′. Active site modeling of dimerization interface in combination with site-directed mutagenesis indicates that the electron in the PrnD Rieske oxygenase can be transferred by either of two pathways, one involving Asp183′ and the other involving Asn180′. In addition, the overexpression of the isc operon involved in the assembly of iron–sulfur clusters increased the catalytic activity of PrnD in Escherichia coli by a factor of at least 4.
ISSN:	0960-894X 1464-3405
DOI:	10.1016/j.bmcl.2011.03.087