Purification and characterization of alkylcatechol 2,3-dioxygenase from butylphenol degradation pathway of Pseudomonas putida MT4
| Autor: | Masahiro Takeo, Seiji Negoro, Dai-ichiro Kato, Hana Takahashi, Chitoshi Kitamura, Munehiro Nishimura |
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| Rok vydání: | 2007 |
| Předmět: |
Alkylation
Molecular Sequence Data Bioengineering Applied Microbiology and Biotechnology Catechol 2 3-Dioxygenase chemistry.chemical_compound Enzyme activator Phenols Species Specificity Dioxygenase Enzyme Stability Amino Acid Sequence chemistry.chemical_classification Catechol biology Pseudomonas putida biology.organism_classification Molecular biology Enzyme Activation Kinetics Enzyme Biodegradation Environmental Biochemistry chemistry Pseudomonadales Bacteria Biotechnology Pseudomonadaceae |
| Zdroj: | Journal of bioscience and bioengineering. 104(4) |
| ISSN: | 1389-1723 |
| Popis: | Alkylcatechol 2,3-dioxygenase was purified from the cell extract of recombinant Escherichia coli JM109 harboring the alkylcatechol 2,3-dioxygenase gene (bupB) cloned from the butylphenol-degrading bacterium Pseudomonas putida MT4. The purified enzyme (BupB) showed relative meta-cleavage activities for the following catechols: catechol (100%), 4-methylcatechol (572%), 4-n-butylcatechol (185%), 4-n-hexylcatechol (53%), 4-n-heptylcatechol (45%), 4-n-nonylcatechol (10%), 4-tert-butylcatechol (0%), and 3-methylcatechol (33%). The kinetic parameters, namely, K(m) and V(max), for catechol, 4-methylcatechol, and 4-n-butylcatechol, were 23.4, 8.4, and 6.5 microM and 25.8, 76.9, and 18.0 U mg(-1), respectively. These results suggest that BupB has broad substrate specificity for 4-n-alkylcatechols. |
| Databáze: | OpenAIRE |
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