Abstract
We have cloned and overexpressed rat 4-hydroxyphenylpyruvate dioxygenase (4HPPD) in Escherichia coli. The soluble, active recombinant enzyme was shown to contain both 4HPPD and α-ketoisocaproate dioxygenase (αKICD) activity. However, upon truncation of the 14 amino acids at the C-terminus by site-directed mutagenesis, the resulting mutant enzyme (rat F antigen) exhibited complete loss of 4HPPD and αKICD activities. This finding suggests that the C-terminal extension domain plays an essential role in the catalytic activity of the enzyme.
| Original language | English |
|---|---|
| Pages (from-to) | 269-272 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 393 |
| Issue number | 2-3 |
| DOIs | |
| Publication status | Published - 16 Sept 1996 |
| Externally published | Yes |
Keywords
- 4-Hydroxyphenylpyruvate dioxygenase
- C-terminal domain
- Rat F antigen
- α-Ketoisocaproate dioxygenase