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

Meng Huee Lee, Zhi Hong Zhang, Colin H. MacKinnon, Jack E. Baldwin, Nicholas P. Crouch*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)


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 languageEnglish
Pages (from-to)269-272
Number of pages4
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 16 Sept 1996
Externally publishedYes


  • 4-Hydroxyphenylpyruvate dioxygenase
  • C-terminal domain
  • Rat F antigen
  • α-Ketoisocaproate dioxygenase

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