Abstract
Protein engineering on trypanosomal triosephosphate isomerase (TIM) converted this oligomeric enzyme into a stable, monomeric protein that is enzymatically active. Wild-type TIM consists of two identical subunits that form a very tight dimer involving interactions of 32 residues of each subunit. By replacing 15 residues of the major interface loop by another 8-residue fragment, a variant was constructed that is a stable and monomeric protein with TIM activity. The length, sequence, and conformation of the designed fragment were suggested by extensive modeling.
Dates
Type | When |
---|---|
Created | 19 years, 2 months ago (May 31, 2006, 9:03 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 1:48 p.m.) |
Indexed | 1 month, 1 week ago (July 19, 2025, 11:21 p.m.) |
Issued | 31 years, 6 months ago (Feb. 15, 1994) |
Published | 31 years, 6 months ago (Feb. 15, 1994) |
Published Online | 31 years, 6 months ago (Feb. 15, 1994) |
Published Print | 31 years, 6 months ago (Feb. 15, 1994) |
@article{Borchert_1994, title={Design, creation, and characterization of a stable,monomeric triosephosphate isomerase.}, volume={91}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.91.4.1515}, DOI={10.1073/pnas.91.4.1515}, number={4}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Borchert, T V and Abagyan, R and Jaenicke, R and Wierenga, R K}, year={1994}, month=feb, pages={1515–1518} }