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 an essential role in the catalytic activity of the enzyme.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 372.4KB, Terms of use)
-
- Publisher copy:
- 10.1016/0014-5793(96)00902-7
Authors
- Publisher:
- Elsevier
- Journal:
- FEBS Letters More from this journal
- Volume:
- 393
- Issue:
- 2-3
- Pages:
- 269-272
- Publication date:
- 1996-09-01
- Edition:
- Publisher's version
- DOI:
- EISSN:
-
9600-9027
- ISSN:
-
0014-5793
- Language:
-
English
- Keywords:
- Subjects:
- UUID:
-
uuid:df40f6c6-9d46-4e7e-823c-a3c1c44d8ef6
- Local pid:
-
ora:8510
- Deposit date:
-
2014-06-03
- ARK identifier:
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