Structure-function analysis of the bacterial aromatic ring-hydroxylating dioxygenases.

Publisher Summary The bacterial aromatic ring-hydroxylating dioxygenases represent a broad range of multi-component enzymes that possess many properties and mechanisms in common. This has enabled their classification based on structural properties. This classification has been supported by sequence comparisons based on nucleotide and primary amino-acid sequences. Comparison of the low homology sequences has also enabled the identification of highly conserved functional motifs—for example iron-sulphur ligation domains—whereas analysis of high homology sequences has allowed the characterization of amino acids involved in more specific functions, such as the control of substrate specificity. This combination of sequence analysis with structure-function studies proves to be invaluable for future protein engineering of improved enzymes for both biocatalysis and environmental remediation. The chapter focuses on the ring-hydroxylating dioxygenases, referring to ring-cleavage dioxygenases and other related systems, and also describes bacterial oxygenases and dioxygenases.

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