Analysis of a new dimeric extradiol dioxygenase from a naphthalenesulfonate-degrading sphingomonad

Article Abstract:

Analysis of the genome of the BN6 naphthalenesulfonate-degrading bacteria indicated the presence of a gene that encoded a novel extradiol dioxygenase (BphC2) that participates in the degradation of naphthalenesulfonates. The BphC2 extradiol dioxygenase from BN6 exhibited an amino-terminal amino acid sequence and a substrate specificity that was distinct from other 1,2-dihydroxynaphthalene dioxygenases. Furthermore, the biochemical activity of the novel extradiol dioxygenase was similar to 2,3-dihydroxybiphenyl dioxygenase.

Oxidases, Microbial enzymes, Bacteria, Aerobic, Aerobic bacteria

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Genetic analysis of biodegradation of tetralin by a Sphingomonas strain

Article Abstract:

A strain labeled TFA and identified as Sphingomonas macrogoltabidus was detected from the mud of the Rhine river. The strain, which is described as a small, short rod-shape, aerobic, gram negative bacterium, was found to effectively use tertralin. Its tertralin biodegradation was genetically analyzed through insertion mutagenesis, physical analysis and complementation analysis between the mutants. Results indicate that the genes responsible for tetralin utilization are those found in its 9 kb region.

Gram-negative bacteria, Biodegradation, Genetic research

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Site-directed mutagenesis of an extradiol dioxygenase involved in tetralin biodegradation identifies residues important for activity or substrate specificity

Article Abstract:

Research delineates the role of some conserved amino acid residues that influence the extradiol dioxygenase enzyme function or substrate specificity by examining number of single amino acid substitution mutants of the enzyme. The mechanism of extradiol dioxygenases imposed substrate inhibition is also examined.

Spain, Physiological aspects, Enzyme structure-activity relationships, Mutagenesis, Amino acid structure-activity relationships, Substitution reactions

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