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

Meng Huee Lee; Zhi Hong Zhang; Colin H. MacKinnon; Jack E. Baldwin; Nicholas P. Crouch

doi:10.1016/0014-5793(96)00902-7

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

Meng Huee Lee, Zhi Hong Zhang, Colin H. MacKinnon, Jack E. Baldwin, Nicholas P. Crouch^*

^*Corresponding author for this work

University of Oxford

Research output: Contribution to journal › Article › peer-review

21 Citations (Scopus)

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 an essential role in the catalytic activity of the enzyme.

Original language	English
Pages (from-to)	269-272
Number of pages	4
Journal	FEBS Letters
Volume	393
Issue number	2-3
DOIs	https://doi.org/10.1016/0014-5793(96)00902-7
Publication status	Published - 16 Sept 1996
Externally published	Yes

Keywords

4-Hydroxyphenylpyruvate dioxygenase
C-terminal domain
Rat F antigen
α-Ketoisocaproate dioxygenase

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10.1016/0014-5793(96)00902-7

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title = "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 an essential role in the catalytic activity of the enzyme.",

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AU - Lee, Meng Huee

AU - Zhang, Zhi Hong

AU - MacKinnon, Colin H.

AU - Baldwin, Jack E.

AU - Crouch, Nicholas P.

PY - 1996/9/16

Y1 - 1996/9/16

N2 - 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.

AB - 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.

KW - 4-Hydroxyphenylpyruvate dioxygenase

KW - C-terminal domain

KW - Rat F antigen

KW - α-Ketoisocaproate dioxygenase

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JO - FEBS Letters

JF - FEBS Letters

IS - 2-3

ER -

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

Abstract

Keywords

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