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Purification and Properties of Hypoxanthine Phosphoribosyltransferase fromStreptomyces cyanogenus
| Content Provider | Scilit |
|---|---|
| Author | Ohe, Tatsuhiko Watanabe, Yasuto |
| Copyright Year | 1980 |
| Description | Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) of a strain of Streptomyces cyanogenus was purified 1,900-fold to an apparent homogenity from cell-free extracts. The enzyme had a molecular weight of 150,000 and consisted of eight identical subunits with a molecular weight of 18,000. The isoelectric point was at pH 4.4. The enzyme required $Mg^{2+}$ or $Ma^{2+}$ for activity and had a pH optimum at 8.5. Hypoxanthine and guanine were good substrates for the enzyme. Xanthine was a very poor substrate and adenine was not a substrate. Apparent Km values of the enzyme for hypoxanthine, guanine and 5-phosphoribose-1-pyro-phosphate were 1.6 × $10^{−8}$, 2.7 × $10^{−6}$ and 6.3 × $10^{−5}$ m, respectively. All purine nucleotides tested inhibited the activity significantly, apparently by competing with 5-phosphoribose-1-pyrophosphate. |
| Related Links | https://www.tandfonline.com/doi/pdf/10.1080/00021369.1980.10864271?needAccess=true |
| Ending Page | 2006 |
| Page Count | 8 |
| Starting Page | 1999 |
| ISSN | 09168451 |
| e-ISSN | 13476947 |
| DOI | 10.1080/00021369.1980.10864271 |
| Journal | Bioscience, Biotechnology, and Biochemistry |
| Issue Number | 9 |
| Volume Number | 44 |
| Language | English |
| Publisher | Informa UK Limited |
| Publisher Date | 1980-09-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Bioscience, Biotechnology, and Biochemistry Microbiology Substrate Adenine Hypoxanthine Phosphoribosyltransferase Isoelectric Fromstreptomyces Cyanogenus Phosphoribose |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Medicine Analytical Chemistry Molecular Biology Biochemistry Applied Microbiology and Biotechnology Biotechnology |
