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...
| Hlavní autoři: | , , , , |
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| Médium: | Journal article |
| Jazyk: | English |
| Vydáno: |
Elsevier
1996
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| Témata: |
| _version_ | 1826300760389844992 |
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| author | Lee, M Zhang, Z MacKinnon, C Baldwin, J Crouch, N |
| author2 | Federation of European Biochemical Societies |
| author_facet | Federation of European Biochemical Societies Lee, M Zhang, Z MacKinnon, C Baldwin, J Crouch, N |
| author_sort | Lee, M |
| collection | OXFORD |
| description | <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> |
| first_indexed | 2024-03-07T05:22:04Z |
| format | Journal article |
| id | oxford-uuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef6 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:22:04Z |
| publishDate | 1996 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef62022-03-27T09:38:09ZThe C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activityJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef6BiochemistryEnglishOxford University Research Archive - ValetElsevier1996Lee, MZhang, ZMacKinnon, CBaldwin, JCrouch, NFederation of European Biochemical Societies<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> |
| spellingShingle | Biochemistry Lee, M Zhang, Z MacKinnon, C Baldwin, J Crouch, N The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title | The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title_full | The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title_fullStr | The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title_full_unstemmed | The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title_short | The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| title_sort | c terminal of rat 4 hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity |
| topic | Biochemistry |
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