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| Content Provider | Springer Nature Link |
|---|---|
| Author | Guzik, Urszula Hupert Kocurek, Katarzyna Sitnik, Małgorzata Wojcieszyńska, Danuta |
| Copyright Year | 2013 |
| Abstract | This is the first report of a catechol 1,2-dioxygenase from Stenotrophomonas maltophilia strain KB2 with high activity against catechol and its methyl derivatives. This enzyme was maximally active at pH 8.0 and 40 °C and the half-life of the enzyme at this temperature was 3 h. Kinetic studies showed that the value of K m and V max was 12.8 μM and 1,218.8 U/mg of protein, respectively. During our studies on kinetic properties of the catechol 1,2-dioxygenase we observed substrate inhibition at >80 μM. The nucleotide sequence of the gene encoding the S. maltophilia strain KB2 catechol 1,2-dioxygenase has high identity with other catA genes from members of the genus Pseudomonas. The deduced 314-residue sequence of the enzyme corresponds to a protein of molecular mass 34.5 kDa. This enzyme was inhibited by competitive inhibitors (phenol derivatives) only by ca. 30 %. High tolerance against condition changes is desirable in industrial processes. Our data suggest that this enzyme could be of use as a tool in production of cis,cis-muconic acid and its derivatives. |
| Starting Page | 1297 |
| Ending Page | 1307 |
| Page Count | 11 |
| File Format | |
| ISSN | 00036072 |
| Journal | Antonie van Leeuwenhoek |
| Volume Number | 103 |
| Issue Number | 6 |
| e-ISSN | 15729699 |
| Language | English |
| Publisher | Springer Netherlands |
| Publisher Date | 2013-03-28 |
| Publisher Place | Dordrecht |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | cis,cis-muconic acid production Stenotrophomonas Catechol 1,2-dioxygenase Substrate specificity Kinetic Microbiology Medical Microbiology Plant Sciences Soil Science & Conservation |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Microbiology |
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