Paradigm for Improving the Catalytic Ability of Industrial Enzymes: Linkage Distortions of Carbohydrates in Complexes with Crystalline Proteins

摘要

Future innovations in applications of industrial enzymes to carbohydrates will require improved knowledge of the mode of action One aspect of enzymatic hydrolysis of saccharides could be a twisting distortion of the bonds between adjacent monosaccharide residues in carbohydrate substrates. If such twists are important, then new enzymes could be engineered that would increase the distortion for faster reaction, One way to learn if such distortion occurs is to survey existing crystalline carbohydrate-protein complexes Unusual twists of linkages at the active site in an enzyme may result from catalysis A related question is whether twisting of the linkage bonds increases the molecular potential energy. For the present work we have tracked the twisting in hundreds of protein-carbohydrate structures and used improved computer modeling of cellobiose to obtain energies, The largest apparent distortions were in similar molecules based on lactose.