author_facet Eltis, L D
Bolin, J T
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Bolin, J T
author Eltis, L D
Bolin, J T
spellingShingle Eltis, L D
Bolin, J T
Journal of Bacteriology
Evolutionary relationships among extradiol dioxygenases
Molecular Biology
Microbiology
author_sort eltis, l d
spelling Eltis, L D Bolin, J T 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.178.20.5930-5937.1996 <jats:p>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.</jats:p> Evolutionary relationships among extradiol dioxygenases Journal of Bacteriology
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title Evolutionary relationships among extradiol dioxygenases
title_unstemmed Evolutionary relationships among extradiol dioxygenases
title_full Evolutionary relationships among extradiol dioxygenases
title_fullStr Evolutionary relationships among extradiol dioxygenases
title_full_unstemmed Evolutionary relationships among extradiol dioxygenases
title_short Evolutionary relationships among extradiol dioxygenases
title_sort evolutionary relationships among extradiol dioxygenases
topic Molecular Biology
Microbiology
url http://dx.doi.org/10.1128/jb.178.20.5930-5937.1996
publishDate 1996
physical 5930-5937
description <jats:p>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.</jats:p>
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author_facet Eltis, L D, Bolin, J T, Eltis, L D, Bolin, J T
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description <jats:p>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.</jats:p>
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spelling Eltis, L D Bolin, J T 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.178.20.5930-5937.1996 <jats:p>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.</jats:p> Evolutionary relationships among extradiol dioxygenases Journal of Bacteriology
spellingShingle Eltis, L D, Bolin, J T, Journal of Bacteriology, Evolutionary relationships among extradiol dioxygenases, Molecular Biology, Microbiology
title Evolutionary relationships among extradiol dioxygenases
title_full Evolutionary relationships among extradiol dioxygenases
title_fullStr Evolutionary relationships among extradiol dioxygenases
title_full_unstemmed Evolutionary relationships among extradiol dioxygenases
title_short Evolutionary relationships among extradiol dioxygenases
title_sort evolutionary relationships among extradiol dioxygenases
title_unstemmed Evolutionary relationships among extradiol dioxygenases
topic Molecular Biology, Microbiology
url http://dx.doi.org/10.1128/jb.178.20.5930-5937.1996