Journal article
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...
Expand abstract
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Version of record, pdf, 372.4KB)
-
- Publisher copy:
- 10.1016/0014-5793(96)00902-7
Why is the content I wish to access not available via ORA?
Bibliographic data (the information relating to research outputs) and full-text items (e.g. articles, theses, reports, etc.) arrive in ORA from several different sources. Unfortunately we are not able to make available the full-text for every research output.
Please contact the ORA team (
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
) if you have queries regarding unavailable content OR if you are aware of a full-text copy we can make available.
Content may be unavailable for the following four reasons
-
Version unsuitable
-
We have not obtained a suitable full-text for a given research output. See this page for more information.
-
Recently completed
-
Sometimes content is held in ORA but is unavailable for a fixed period of time to comply with the policies and wishes of rights holders.
-
Permissions
-
All content made available in ORA should comply with relevant rights, such as copyright. See this page for more information.
-
Clearance
-
Some thesis volumes scanned as part of the digitisation scheme funded by Dr Leonard Polonsky are currently unavailable due to sensitive material or uncleared third-party copyright content. We are attempting to contact authors whose theses are affected.
Alternative access to the full-text
You may be able to access the full-text directly from the publisher's website using the 'Publisher Copy' link in the 'Links & Downloads' box from a research output's ORA record page. This method may require an institutional or individual subscription to the journal/resource.
Bibliographic Details
- Publisher:
- Elsevier Publisher's website
- Journal:
- FEBS Letters Journal website
- Volume:
- 393
- Issue:
- 2-3
- Pages:
- 269-272
- Publication date:
- 1996-09-01
- DOI:
- EISSN:
-
9600-9027
- ISSN:
-
0014-5793
Item Description
- Language:
- English
- Keywords:
- Subjects:
- UUID:
-
uuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef6
- Local pid:
- ora:8510
- Deposit date:
- 2014-06-03
Related Items
Terms of use
- Copyright holder:
- Federation of European Biochemical Societies
- Copyright date:
- 1996
- Notes:
- Copyright 1996 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. Re-use of this article is permitted in accordance with the Terms and Conditions set out at http://www.elsevier.com/open-access/userlicense/1.0/
- Licence:
- Other
If you are the owner of this record, you can report an update to it here: Report update to this record