期刊论文详细信息
FEBS Letters
The C‐terminal of rat 4‐hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity
Crouch, Nicholas P.1  Zhang, Zhi-Hong1  MacKinnon, Colin H.1  Baldwin, Jack E.1  Lee, Meng-Huee1 
[1] The Dyson Perrins Laboratory and The Oxford Center for Molecular Sciences, South Parks Road, University of Oxford, Oxford, OX1 3QY, UK
关键词: 4-Hydroxyphenylpyruvate dioxygenase;    α-Ketoisocaproate dioxygenase;    Rat F antigen;    C-terminal domain;    DTT;    dithiothreitol;    4HPP;    4-hydroxyphenylpyruvate;    4HPPD;    4-hydroxyphenylpyruvate dioxygenase;    αKIC;    α-ketoisocaproate;    αKICD;    α-ketoisocaproate dioxygenase;    RFA;    rat F antigen;   
DOI  :  10.1016/0014-5793(96)00902-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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.

【 授权许可】

Unknown   

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