Phosphopentomutase ofBacillus stearothermophilusTH6-2: The Enzyme and Its Geneppm
| Autor: | Tomoki Hamamoto, Toshitada Noguchi, Yuichiro Midorikawa |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Molecular Sequence Data
Restriction Mapping Gene Expression Purine nucleoside phosphorylase Isomerase Biology Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Analytical Chemistry Geobacillus stearothermophilus Gene product Open Reading Frames chemistry.chemical_compound Ribose Escherichia coli Nucleotide Amino Acid Sequence Molecular Biology chemistry.chemical_classification Base Sequence Sequence Homology Amino Acid Phosphotransferases Organic Chemistry General Medicine Phosphopentomutase Recombinant Proteins Molecular Weight Deoxyribose chemistry Genes Bacterial Nucleoside Plasmids Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 62:1103-1108 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.62.1103 |
| Popis: | Phosphopentomutase catalyzes the transfer of an intramolecular phosphate on ribose or deoxyribose, and is involved in the salvage pathway of nucleoside synthesis. We identified a sequence 5'-upstream of the genes for the nucleoside phosphorylases of Bacillus stearothermophilus as the phosphopentomutase (ppm) gene. The novel gene corresponded to an open reading frame of 1,179 nucleotides that is translated into a putative 393-amino acid protein with a molecular weight of 43,735. The gene product, partially purified from ppm-overexpressing Escherichia coli cells, was judged to be a monomer of a 44-kDa polypeptide. The phosphopentomutase was found to catalyze the phosphotransfer on not only ribose or deoxyribose but also arabinose or dideoxyribose. |
| Databáze: | OpenAIRE |
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