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

Authors: Lee, MH  Zhang, ZH  MacKinnon, CH  Baldwin, JE  Crouch, NP 
Citation: Lee MH, etal., FEBS Lett. 1996 Sep 16;393(2-3):269-72.
Pubmed: (View Article at PubMed) PMID:8814303

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.

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CRRD Object Information
CRRD ID: 8554707
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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