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The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity.

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.[1]

References

  1. The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity. Lee, M.H., Zhang, Z.H., MacKinnon, C.H., Baldwin, J.E., Crouch, N.P. FEBS Lett. (1996) [Pubmed]
 
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