EpsN from Bacillus subtilis 168 has UDP-2,6-dideoxy 2-acetamido 4-keto glucose aminotransferase activity in vitro
| Autor: | K. Krishnamurthy Rao, Chinmayi R. Kaundinya, Handanahal S. Savithri, Petety V. Balaji |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Bacillus subtilis medicine.disease_cause Biochemistry Uridine Diphosphate law.invention 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins law medicine Gene Escherichia coli Pyridoxal Transaminases Schiff base biology Molecular Structure Mutagenesis Polysaccharides Bacterial biology.organism_classification In vitro Recombinant Proteins carbohydrates (lipids) 030104 developmental biology Glucose chemistry Recombinant DNA Biocatalysis Mutagenesis Site-Directed |
| Zdroj: | Glycobiology. 28(10) |
| ISSN: | 1460-2423 |
| Popis: | The gene epsN of Bacillus subtilis 168 was cloned and overexpressed in Escherichia coli. Purified recombinant EpsN is shown to be a pyridoxal 5'-phosphate (PLP)-dependent aminotransferase by absorption spectroscopy, L-cycloserine inhibition and reverse phase HPLC studies. EpsN catalyzes the conversion of UDP-2,6-dideoxy 2-acetamido 4-keto glucose to UDP-2,6-dideoxy 2-acetamido 4-amino glucose. Lys190 was found by sequence comparison and site-directed mutagenesis to form Schiff base with PLP. Mutagenesis studies showed that, in addition to Lys190, Ser185, Glu164, Gly58 and Thr59 are essential for aminotransferase activity. |
| Databáze: | OpenAIRE |
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