Cryoenzymology: Enzyme Action in Slow Motion
Document Type
Article
Publication Date
2009
Keywords
Enzyme, Catalysis, Cryoenzymology, Enzymology
Digital Object Identifier (DOI)
https://doi.org/10.2174/138920309789351958
Abstract
Knowledge of the existence and structure of intermediates on the reaction pathway is necessary before specific details of the mechanism may be successfully resolved. However, enzymatic catalysis is an extremely fast process. This rapidity of enzyme-catalyzed reactions and the short life times of intermediates represent a major problem in studying the dynamic processes which occur during catalysis, as they prevent the accumulation of intermediates under normal conditions for concentrations and time periods required by most high-resolution structural methods. Therefore, a method that would utilize specific substrates but would permit the detection and characterization of intermediates was highly desired. As one of the approaches to overcome this problem the use of cryoenzymology to allow the accumulation and stabilization of intermediates at very low temperatures was proposed. This review describes the contribution of Prof. Anthony L. Fink to cryoenzymology and shows how his work shaped this exciting area.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Current Protein and Peptide Science, v. 10, issue 5, p. 408-415
Scholar Commons Citation
Dunn, Ben M. and Uversky, Vladimir N., "Cryoenzymology: Enzyme Action in Slow Motion" (2009). Molecular Medicine Faculty Publications. 566.
https://digitalcommons.usf.edu/mme_facpub/566
