ABSTRACT
Rhodococcus sp. NCIMB112038 can utilize naphthalene as its sole carbon and energy source. The gene encoding cis-naphthalene dihydrodiol dehydrogenase (narB) of this strain has been cloned and sequenced. Expression of NCIMB12038 cis-naphthalene dihydrodiol dehydrogenase was demonstrated in Escherichia coli cells. narB encodes a putative protein of 271 amino acids and shares 39% amino acid identity with the cis-naphthalene dihydrodiol dehydrogenase from Pseudomonas putida G7. Comparison of NarB with some putative cis-dihydrodiol dehydrogenases from Rhodococcus species revealed significant differences between these proteins. NarB together with two other proteins forms a new group of cis-dihydrodiol dehydrogenases.
Subject(s)
Alcohol Oxidoreductases/genetics , Alcohol Oxidoreductases/metabolism , Naphthalenes/metabolism , Oxidoreductases Acting on CH-CH Group Donors , Oxidoreductases , Rhodococcus/enzymology , Rhodococcus/genetics , Alcohol Oxidoreductases/chemistry , Amino Acid Sequence , Biodegradation, Environmental , Cell Fractionation , Cloning, Molecular , Culture Media , Genes, Bacterial , Molecular Sequence Data , Phylogeny , Rhodococcus/growth & development , Sequence Alignment , Sequence Analysis, DNAABSTRACT
We report here the characterization of the catalytic component (ISP(NAR)) of a new naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038. The genes encoding the two subunits of ISP(NAR) are not homologous to their previously characterized counterparts in Pseudomonas. The deduced amino acid sequences have only 33 and 29% identity with the corresponding subunits in Pseudomonas putida NCIB 9816-4, for which the tertiary structure has been reported.
