Recombinant curculin heterodimer exhibits taste‐modifying and sweet‐tasting activities
- 9 August 2004
- journal article
- clinical trial
- Published by Wiley in FEBS Letters
- Vol. 573 (1-3), 135-138
- https://doi.org/10.1016/j.febslet.2004.07.073
Abstract
Curculin from Curculigo latifolia is a unique sweet protein that exhibits both sweet-tasting and taste-modifying activities. We isolated a gene that encodes a novel protein highly homologous to curculin. Using cDNAs of the previously known curculin (designated as curculin1) and the novel curculin isoform (curculin2), we produced a panel of homodimeric and heterodimeric recombinant curculins by Escherichia coli expression systems. It was revealed that sweet-tasting and taste-modifying activities were exhibited solely by the heterodimer of curculin1 and curculin2This publication has 19 references indexed in Scilit:
- Interaction of sweet proteins with their receptorJBIC Journal of Biological Inorganic Chemistry, 2004
- Probing the surface of a sweet protein: NMR study of MNEI with a paramagnetic probeProtein Science, 2001
- Solution Structure, Backbone Dynamics, and Stability of a Double Mutant Single-chain MonellinOnline Journal of Public Health Informatics, 2001
- Solution structure of a sweet protein: NMR study of MNEI, a single chain monellinJournal of Molecular Biology, 2001
- Activity and Stability of a New Sweet Protein with Taste-modifying Action, CurculinChemical Senses, 1995
- Two Crystal Structures of a Potently Sweet Protein: Natural Monellin at 2·75 Å Resolution and Single-Chain Monellin at 1·7 Å ResolutionJournal of Molecular Biology, 1993
- Crystal structure of a sweet tasting protein thaumatin I, at 1·65 Å resolutionJournal of Molecular Biology, 1992
- Crystal structure of the intensely sweet protein monellinNature, 1987
- Isolation of mammalian messenger ribonucleic acidBiochemistry, 1972