Flow catalysis makes the cooperation possible ... were thus converted into trehalose in two steps that took place on immobilised enzymes. The first enzyme has the task of activating the glucose ...

In the first step, the p-nitrophenyl group is released quickly but the acetate group remains covalently bound to the enzyme. In a second, slower step, the enzyme reacts with water and the acetate ...

In biology, enzymes have evolved over millions of years to drive chemical reactions. Scientists from the Max Planck Institute ...

The Post group has worked to understand the basis of the catalytic power of enzymes using information from crystallography, kinetics, and a description of conformational distributions from molecular ...

Lalonde: Biocatalysis is considered to be greener than transition metal catalysis in some key regards ... activation, or deprotection steps), enzymes for regiospecific glycosylation of hydroxyl groups ...

Water molecules play a number of critical roles in enzyme catalysis, including mass transfer of substrates and products, nucleophilicity and proton transfer at the active site, and solvent shell ...

More information: Xiaofei Zhang et al, Creating enzyme-mimicking nanopockets in metal-organic frameworks for catalysis, Science Advances (2022). DOI: 10.1126/sciadv.add5678 Journal information ...

Enzyme catalysis, which uses biological proteins to accelerate chemical reactions has emerged as a sustainable approach to make chiral molecules. However, using proteins as catalysts poses challenges, ...