| First Author | Lee MH | Year | 1996 |
| Journal | FEBS Lett | Volume | 393 |
| Issue | 2-3 | Pages | 269-72 |
| PubMed ID | 8814303 | Mgi Jnum | J:35374 |
| Mgi Id | MGI:82823 | Doi | 10.1016/0014-5793(96)00902-7 |
| Citation | Lee MH, et al. (1996) The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity. FEBS Lett 393(2-3):269-72 |
| abstractText | 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 alpha-ketoisocaproate dioxygenase (alpha KICD) 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 alpha KICD activities. This finding suggests that the C-terminal extension domain plays an essential role in the catalytic activity of the enzyme. |
