The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Evolutionary relationships among extradiol dioxygenases
Open accessAbstract
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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Metadata
- Authors
- Eltis, L. D., & Bolin, J. T.
- Venue
- Journal of Bacteriology
- Publisher
- American Society for Microbiology
- Published
- 1996-10
- Volume
- 178
- Issue
- 20
- Pages
- 5930-5937
- ISSN
- 0021-9193 (ISSN-L)
- 1098-5530
- OpenAlex
- W1929452298
- Cited by
- 289
- References
- 20
- FWCI
- 12.30
- Type
- journal article
- Language
- en
- Open access
- green
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