Bioscience, biotechnology, and biochemistry, 2008-12, Vol.72 (12), p.3237-3248
2008
Details
- Autor(en) / Beteiligte
- Titel
- Alteration of the substrate specificity of the angular dioxygenase carbazole 1,9a-dioxygenase
- Ist Teil von
- Bioscience, biotechnology, and biochemistry, 2008-12, Vol.72 (12), p.3237-3248
- Ort / Verlag
- Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry
- Erscheinungsjahr
- 2008
- Link zum Volltext
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Carbazole 1,9a-dioxygenase (CARDO) consists of terminal oxygenase (CARDO-O) and electron transport components. CARDO can catalyze specific oxygenation for various substrates: angular dioxygenation for carbazole and dibenzo-p-dioxin, lateral dioxygenation for anthracene, and monooxygenation for methylene carbon of fluorene and sulfide sulfur of dibenzothiophene. To elucidate the molecular mechanism determining its unique substrate specificity, 17 CARDO-O site-directed mutants at amino acid residues I262, F275, Q282, and F329, which form the substrate-interacting wall around the iron active site by CARDO-O crystal structure, were generated and characterized. F329 replacement dramatically reduced oxygenation activity. However, several mutants produced different products from the wild-type enzyme to a large extent: I262V and Q282Y (1-hydroxycarbazole), F275W (4-hydroxyfluorene), F275A (unidentified cis-dihydrodiol of fluoranthene), and I262A and I262W (monohydroxydibenzothiophenes). These results suggest the possibility that the respective substrates bind to the active sites of CARDO-O mutants in a different orientation from that of the wild-type enzyme.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0916-8451eISSN: 1347-6947DOI: 10.1271/bbb.80512Titel-ID: cdi_proquest_miscellaneous_20385671
- Format
- –
- Schlagworte
- angular dioxygenation, Anthracenes - metabolism, AROMATIC COMPOUNDS, Bacterial Proteins - chemistry, Bacterial Proteins - genetics, Bacterial Proteins - metabolism, BIOCHEMICAL ENGINEERING, BIOCHEMICAL REACTIONS, Biological and medical sciences, carbazole 1,9a-dioxygenase, Carbazoles - metabolism, Catalytic Domain, COMPOSE AROMATIQUE, COMPUESTOS AROMATICOS, Dioxins - metabolism, Dioxygenases - chemistry, Dioxygenases - genetics, Dioxygenases - metabolism, Escherichia coli - cytology, Escherichia coli - metabolism, Fluorenes - metabolism, Fundamental and applied biological sciences. Psychology, GENIE BIOCHIMIQUE, INGENIERIA BIOQUIMICA, Models, Molecular, MUTACION, Mutagenesis, Site-Directed, MUTATION, Oxidation-Reduction, OXIDOREDUCTASES, OXIDORREDUCTASAS, OXYDOREDUCTASE, Protein Conformation, REACCIONES BIOQUIMICAS, REACTION BIOCHIMIQUE, Rieske non-heme iron oxygenase, site-directed mutagenesis, SUBSTANCE TOXIQUE, Substrate Specificity, SUSTANCIAS TOXICAS, Thiophenes - metabolism, TOXIC SUBSTANCES