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| Content Provider | Springer Nature Link |
|---|---|
| Author | Semenihina, A. Popova, T. Schnarrenberger, C. Pinheiro De Carvalho, M.A.A. |
| Copyright Year | 2001 |
| Abstract | The cytosolic and chloroplastic isoforms of glucose-6-phosphate dehydrogenase (G$_{6}$PDH) were separated and purified from barley leaves (Hordeum vulgare L.). In etiolated leaves, only the cytosolic isoform was expressed. The molecular mass of the cytosolic enzyme, G$_{6}$PDH$_{1}$, was 112±8 kDa and that of the chloroplast enzyme, G$_{6}$PDH$_{2}$, was 136±7 kDa. The K$_{m}$ values for glucose-6-phosphate and NADP were 0.133 and 0.041 mM for G$_{6}$PDH$_{1}$, and 0.275 and 0.062 mM for G$_{6}$PDH$_{2}$, respectively. The pH optimum was 8.2 for G$_{6}$PDH$_{1}$ and 7.8 for G$_{6}$PDH$_{2}$. The enzyme is absolutely specific for NADP. NADPH is a competitive inhibitor of the G$_{6}$PDH$_{1}$ in respect to glucose-6-phosphate (G$_{6}$P) and NADP (K$_{i}$ = 0.050 and 0.025 mM, respectively). NADPH is a competitive inhibitor of the G$_{6}$PDH$_{2}$ in respect to NADP (K$_{i}$ = 0.010 mM), but a non-competitive inhibitor in respect to the G$_{6}$P. ADP, AMP, UTP, NAD, and NADH had no effect on the activity of G$_{6}$PDH. ATP inhibited the G$_{6}$PDH$_{2}$ activity. |
| Starting Page | 299 |
| Ending Page | 304 |
| Page Count | 6 |
| File Format | |
| ISSN | 03003604 |
| Journal | Photosynthetica |
| Volume Number | 39 |
| Issue Number | 2 |
| e-ISSN | 15739058 |
| Language | English |
| Publisher | Kluwer Academic Publishers |
| Publisher Date | 2001-01-01 |
| Publisher Place | Dordrecht |
| Access Restriction | Subscribed |
| Subject Keyword | Plant Physiology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Plant Science |
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