Triosephosphate Isomerase: A Theoretical Comparison of Alternative Pathways
Author:
Affiliation:
1. Contribution from the Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, Laboratoire de Chimie Biophysique, ISIS, Université Louis Pasteur, 67000 Strasbourg France
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja002886c
Reference27 articles.
1. Enzyme catalysis: not different, just better
2. Energetics of triosephosphate isomerase: the fate of the 1(R)-3H label of tritiated dihydroxyacetone phosphate in the isomerase reaction
3. Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analog of the intermediate on the reaction pathway
4. Neutral imidazole is the electrophile in the reaction catalyzed by triosephosphate isomerase: structural origins and catalytic implications
5. Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
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