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

FEBS Letters

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.

【 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