Aug, 2005
The role of firefly luciferase C-terminal domain in efficient coupling of adenylation and oxidative steps
FEBS LETTERS
- ,
- ,
- Volume
- 579
- Number
- 20
- First page
- 4389
- Last page
- 4394
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/j.febslet.2005.07.004
- Publisher
- ELSEVIER SCIENCE BV
The N-terminal domain (N-domain) of the firefly luciferase from Photinus pyraris has weak luminescence activity, and shows a unique light emitting profile with very long rise time of more than several minutes. Through a sensitive assay of the reaction intermediate luciferyl-adenylate (LH2-AMP), we found that the slow increase in the N-domain luminescence faithfully reflected the concentration of dissociated LH2-AMP. No such correlation was observed for wild-type or mutant enzymes with short rise time, except one with longer rise time. The results suggest that the C-terminal domain plays an indispensable role in efficiently coupling adenylation and oxidative steps. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
- Link information
-
- DOI
- https://doi.org/10.1016/j.febslet.2005.07.004
- CiNii Articles
- http://ci.nii.ac.jp/naid/30002590919
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/16061229
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000231350900031&DestApp=WOS_CPL
- ID information
-
- DOI : 10.1016/j.febslet.2005.07.004
- ISSN : 0014-5793
- CiNii Articles ID : 30002590919
- Pubmed ID : 16061229
- Web of Science ID : WOS:000231350900031