752993-28-5Relevant academic research and scientific papers
Combined catalytic conversion involving an enzyme, a homogeneous and a heterogeneous catalyst: One-pot preparation of 4-deoxy-D-glucose derivatives from D-galactose
Schoevaart, Rob,Kieboom, Tom
, p. 3399 - 3400 (2002)
Consecutive catalytic oxidation (oxygen, D-galactose oxidase), dehydration (L-proline) and reduction (hydrogen, palladium) of methyl β-D-galactoside in water at neutral pH yielded methyl 4-deoxy-6-aldehydo-β-D-glucoside without intermediate recovery steps demonstrating the potential power of a multi-catalytic approach, using both bio- and chemo-catalysts, for carbohydrate conversions without the use of protective groups or stoichiometric amounts of reagents.
Chemical Mapping Exposes the Importance of Active Site Interactions in Governing the Temperature Dependence of Enzyme Turnover
Winter, Samuel D.,Jones, Hannah B. L.,R?s?dean, Dora M.,Crean, Rory M.,Danson, Michael J.,Panto?, G. Dan,Katona, Gergely,Prentice, Erica,Arcus, Vickery L.,van der Kamp, Marc W.,Pudney, Christopher R.
, p. 14854 - 14863 (2021/12/09)
Uncovering the role of global protein dynamics in enzyme turnover is needed to fully understand enzyme catalysis. Recently, we have demonstrated that the heat capacity of catalysis, ΔCP?, can reveal links between the protein free energy landscape, global protein dynamics, and enzyme turnover, suggesting that subtle changes in molecular interactions at the active site can affect long-range protein dynamics and link to enzyme temperature activity. Here, we use a model promiscuous enzyme (glucose dehydrogenase from Sulfolobus solfataricus) to chemically map how individual substrate interactions affect the temperature dependence of enzyme activity and the network of motions throughout the protein. Utilizing a combination of kinetics, red edge excitation shift (REES) spectroscopy, and computational simulation, we explore the complex relationship between enzyme–substrate interactions and the global dynamics of the protein. We find that changes in ΔCP? and protein dynamics can be mapped to specific substrate–enzyme interactions. Our study reveals how subtle changes in substrate binding affect global changes in motion and flexibility extending throughout the protein.
