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The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity
M H Lee1, Z H Zhang, C H MacKinnon
1Dyson Perrins Laboratory, University of Oxford, UK.
FEBS Letters
|September 16, 1996
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 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.