A mechanistic study on SMOB-ADP1: an NADH:flavin oxidoreductase of the two-component styrene monooxygenase of Acinetobacter baylyi ADP1
| Autor: | Dirk Tischler, Stefan R. Kaschabek, Janosch A. D. Gröning, Michael Schlömann |
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| Rok vydání: | 2014 |
| Předmět: |
FMN Reductase
Molecular Sequence Data Flavin group Biology Reductase Biochemistry Microbiology Fusion gene Pseudomonas FMN reductase Genetics Amino Acid Sequence Molecular Biology Gene Phylogeny Acinetobacter Phylogenetic tree General Medicine NAD biology.organism_classification Turnover number Biocatalysis Oxygenases Oxidoreductases |
| Zdroj: | Archives of Microbiology. 196:829-845 |
| ISSN: | 1432-072X 0302-8933 |
| Popis: | Two styrene monooxygenase types, StyA/StyB and StyA1/StyA2B, have been described each consisting of an epoxidase and a reductase. A gene fusion which led to the chimeric reductase StyA2B and the occurrence in different phyla are major differences. Identification of SMOA/SMOB-ADP1 of Acinetobacter baylyi ADP1 may enlighten the gene fusion event since phylogenetic analysis indicated both proteins to be more related to StyA2B than to StyA/StyB. SMOB-ADP1 is classified like StyB and StyA2B as HpaC-like reductase. Substrate affinity and turnover number of the homo-dimer SMOB-ADP1 were determined for NADH (24 µM, 64 s−1) and FAD (4.4 µM, 56 s−1). SMOB-ADP1 catalysis follows a random sequential mechanism, and FAD fluorescence is quenched upon binding to SMOB-ADP1 (K d = 1.8 µM), which clearly distinguishes that reductase from StyB of Pseudomonas. In summary, this study confirmes made assumptions and provides phylogenetic and biochemical data for the differentiation of styrene monooxygenase-related flavin reductases. |
| Databáze: | OpenAIRE |
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