| Autor: |
Hensel, Reinhard, Laumann, Silvia, Lang, Jutta, Heumann, Herrmann, Lottspeich, Friedrich |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 12/30/87, Vol. 170 Issue 1/2, p325-333, 9p |
| Abstrakt: |
Thermoproteus tenax possesses two different glyceraldehyde-3-phosphate dehyerogenases, one specific for NADP+ and the other for NAD+ NADP(H) inhibits the NAD + specific enzyme competetively with respect to NAD + whereas NAD(H) virtually does not interact with the NADP+ specific enzyme. Both enzymes represent homomeric tetramers with subunit molecular masses of 39 kDa (NADP + specific enzyme) and 49 kDa (NAD + - specific enzyme), respectively. The NADP -specific enzyme shows significant homology to the known glyceraldehyde-3-phosphate dehydroa genases from eubacteria and eukaryotes as indicated by partial sequencing. The enzymes are thermostable, the NADP + especific enzyme with a half-life of 35 min at 100°C, the NAD + specific enzyme with a half-line of ⩾ 20 min at 100°C, depending on the protein concentration. Both enzymes show conformational and functional changes at 60-70°C. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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