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

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 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 a...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/0014-5793(96)00902-7

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Institution:
University of Oxford
Role:
Author
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Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
More by this author
Institution:
University of Oxford
Role:
Author
Publisher:
Elsevier B.V. Publisher's website
Journal:
FEBS Letters Journal website
Volume:
393
Issue:
2-3
Pages:
269-272
Publication date:
1996-09-05
DOI:
EISSN:
9600-9027
ISSN:
0014-5793
URN:
uuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef6
Local pid:
ora:8510

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