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J. Bacteriol., Oct 1996, 5930-5937, Vol 178, No. 20
Copyright © 1996, American Society for Microbiology

Evolutionary relationships among extradiol dioxygenases

LD Eltis and JT Bolin
Department of Biochemistry, Universite Laval, Quebec City, Canada. leltis@rsvs.ulaval.ca

A structure-validated alignment of 35 extradiol dioxygenase sequences including two-domain and one-domain enzymes was derived. Strictly conserved residues include the metal ion ligands and several catalytically essential active site residues, as well as a number of structurally important residues that are remote from the active site. Phylogenetic analyses based on this alignment indicate that the ancestral extradiol dioxygenase was a one-domain enzyme and that the two-domain enzymes arose from a single genetic duplication event. Subsequent divergence among the two-domain dioxygenases has resulted in several families, two of which are based on substrate preference. In several cases, the two domains of a given enzyme express different phylogenies, suggesting the possibility that such enzymes arose from the recombination of genes encoding different dioxygenases. A phylogeny- based classification system for extradiol dioxygenases is proposed.


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