Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

Manish Kumar Tiwari; Jung-Kul Lee; Hee-Jung Moon; Huimin Zhao

doi:10.1016/j.bmcl.2011.03.087

Further biochemical studies on aminopyrrolnitrin oxygenase (PrnD)

Bioorg Med Chem Lett. 2011 May 15;21(10):2873-6. doi: 10.1016/j.bmcl.2011.03.087. Epub 2011 Mar 30.

Authors

Manish Kumar Tiwari¹, Jung-Kul Lee, Hee-Jung Moon, Huimin Zhao

Affiliation

¹ Department of Chemical Engineering, Konkuk University, Seoul 143-701, Republic of Korea.

PMID: 21507634
DOI: 10.1016/j.bmcl.2011.03.087

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amines / chemistry*
Binding Sites
Electrophoresis, Polyacrylamide Gel
Escherichia coli / enzymology*
Models, Molecular
Mutagenesis, Site-Directed
Oxygenases / chemistry*
Oxygenases / genetics
Pyrrolnitrin / chemistry*

Substances

Amines
Oxygenases
Pyrrolnitrin