Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 469, Issue 4, Pages 1129-1132Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.12.121
Keywords
ATP binding; ATP synthase; Biosensor; Inhibitor; Protein engineering
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Funding
- JSPS KAKENHI [23770157, 15K07013]
- Ministry of Education, Culture, Sports, Science and Technology of Japan [S1201003]
- Grants-in-Aid for Scientific Research [23770157, 15K07013] Funding Source: KAKEN
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Specific ATP binding to the epsilon subunit of thermophilic F-1-ATPase has been utilized for the biosensors of ATP in vivo. I report here that the epsilon subunit containing R103A/R115A mutations can bind ATP with a dissociation constant at 52 nM, which is two orders of magnitude higher affinity than the wild type. The mutant retained specificity for ATP; ADP and GTP bound to the mutant with dissociation constants 16 and 53 mu M, respectively. Thus, the mutant would be a good platform for various types of nucleotide biosensor with appropriate modifications. (C) 2015 Elsevier Inc. All rights reserved.
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