Biochemical and Genetic Characterization of a Gentisate 1,2-Dioxygenase from Sphingomonas sp. Strain RW5
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Summary
A 4,103-bp long DNA fragment containing the structural gene of a gentisate 1,2-dioxygenase, which appears to be a homotetrameric protein, was subcloned and hyperexpressed in E. coli and purified to homogeneity and partially characterized.
- Type
- article
- Published
- 1998-08-15
- Cited by
- 67
- References
- 52
- OpenAlex
- https://openalex.org/W9696766
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:20645998
Keywords
Medicine
References
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- Evolutionary relationships among extradiol dioxygenases
- The biphenyl/polychlorinated biphenyl-degradation locus (bph) of Pseudomonas sp. LB400 encodes four additional metabolic enzymes.
- A bacterial enzyme degrading the model lignin compound β‐etherase is a member of the glutathione‐S‐transferase superfamily
- Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368.
- Microbial metabolism of xenobiotics: Fundamental and applied research
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- 4-chlorophenol biodegradation by Arthrobacter chlorophenolicus A6
- Function of different amino acid residues in the reaction mechanism of gentisate 1,2-dioxygenases deduced from the analysis of mutants of the salicylate 1,2-dioxygenase from Pseudaminobacter salicylatoxidans.
- SOLATION AND CHARACTERIZATION OF A NOVEL BENZOATE- UTILIZING Serratia marcescens
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- Molecular characterization of an inducible gentisate 1,2-dioxygenase gene, xlnE, from Pseudomonas alcaligenes NCIMB 9867.
- Metabolic Diversity in Bacterial Degradation of Aromatic Compounds
- Biodegradation of dimethylphenols by bacteria with different ring-cleavage pathways of phenolic compounds
- Role of oxygenases in guiding diverse metabolic pathways in the bacterial degradation of low-molecular-weight polycyclic aromatic hydrocarbons: A review
- Transcriptome and membrane fatty acid analyses reveal different strategies for responding to permeating and non-permeating solutes in the bacterium Sphingomonas wittichii
- Biochemical and Molecular Characterization of a Ring Fission Dioxygenase with the Ability to Oxidize (Substituted) Salicylate(s) from Pseudaminobacter salicylatoxidans*
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