The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity
<p>We have cloned and overexpressed rat 4-hydroxyphenylpyruvate dioxygenase (4HPPD) in <em>Escherichia coli</em>. The soluble, active recombinant enzyme was shown to contain both 4HPPD and α-ketoisocaproate dioxygenase (αKICD) activity. However, upon truncation of the 14 amino acid...
| Autori principali: | , , , , |
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| Altri autori: | |
| Natura: | Journal article |
| Lingua: | English |
| Pubblicazione: |
Elsevier
1996
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| Riassunto: | <p>We have cloned and overexpressed rat 4-hydroxyphenylpyruvate dioxygenase (4HPPD) in <em>Escherichia coli</em>. 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.</p> |
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