Cloning of Purine Nucleoside Phosphorylase II Gene fromBacillus stearothermophilusTH 6–2 and Characterization of Its Gene Product
| Autor: | Yuichiro Midorikawa, Tomoki Hamamoto, Toshitada Noguchi |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
DNA
Bacterial Purine Recombinant Fusion Proteins Molecular Sequence Data Guanosine Purine nucleoside phosphorylase Biology medicine.disease_cause Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Analytical Chemistry Geobacillus stearothermophilus Gene product chemistry.chemical_compound Bacterial Proteins Escherichia coli medicine Amino Acid Sequence Isoelectric Point Cloning Molecular Inosine Molecular Biology Phosphorolysis chemistry.chemical_classification Base Sequence Organic Chemistry Temperature Sequence Analysis DNA General Medicine Molecular biology Molecular Weight Enzyme Purine-Nucleoside Phosphorylase chemistry Genes Bacterial Biotechnology medicine.drug |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 61:276-280 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.61.276 |
| Popis: | Bacillus stearothermophilus TH 6-2 has two kinds of purine nucleoside phosphorylases (Pu-NPases). The type I enzyme (Pu-NPase I) is a functional and structural homolog of eukaryotic purine nucleoside phosphorylases that catalyze the phosphorolysis of inosine, guanosine, and their derivatives. The type II enzyme (Pu-NPase II) is a minor enzyme that efficiently phosphorolyzes adenosine and its derivatives rather than other purine nucleosides like Escherichia coli Pu-NPase. The gene coding for Pu-NPase II (punB gene) has been cloned and sequenced from TH 6-2 strain. The deduced amino acid sequence of Pu-NPase II shared 54% identity with that of E. coli enzyme, while it had no significant homology to that of Pu-NPase I or eukaryotic enzymes. By producing the Pu-NPase II in E. coli cells, the Pu-NPase II has been purified and characterized. |
| Databáze: | OpenAIRE |
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