Abstract
Purified nitrate reductase (NR) from spinach leaves was phosphorylated in vitro by NR-inactivating kinase on Ser-543 which is located in the hinge 1 region between the molybdenum-cofactor and haem-binding domains, Phosphorylation of Ser-543 allowed NR to be inhibited by the inhibitor, NIP, Degraded NR preparations in which a proportion of the subunits had lost 45 amino acids from the N-terminus during purification could be phosphorylated by NR kinase on Ser-543, but could not subsequently be fully inhibited by NIP, suggesting a role for the N-terminal tail of NR in NIP binding.
| Original language | English |
|---|---|
| Pages (from-to) | 113-117 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 377 |
| Issue number | 2 |
| Publication status | Published - 1995 |
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