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Title of Journal: J IND MICROBIOL BIOTECHNOL

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Abbravation: Journal of Industrial Microbiology and Biotechnology

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Springer-Verlag

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DOI

10.1016/0360-3016(92)90054-l

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1476-5535

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The role of activesite residues in naphthalene di

Authors: Rebecca E Parales
Publish Date: 2003/04/15
Volume: 30, Issue: 5, Pages: 271-278
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Abstract

The threecomponent naphthalene dioxygenase enzyme system catalyzes the first step in the degradation of naphthalene by Pseudomonas sp strain NCIB 98164 A member of a large family of bacterial Rieske nonheme iron oxygenases naphthalene dioxygenase is known to oxidize over 60 different aromatic compounds and many of the products are enantiomerically pure The crystal structure of the oxygenase component revealed the enzyme to be an α3β3 hexamer and identified the amino acids located near the active site Sitedirected mutagenesis studies have identified the residues involved in electron transfer and those responsible for controlling the regioselectivity and enantioselectivity of the enzyme The results of these studies suggest that naphthalene dioxygenase can be engineered to catalyze a new and extended range of useful reactions


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