Linked from

The 36 pages that link to Enzyme catalysis, each with the reason it gives.

• StereochemistryNarrower topic: Enzymes' three-dimensional active sites often distinguish substrates by stereochemistry.

• Proton transferNarrower topic: Many enzymes use nearby amino-acid residues to shuttle protons between reactants.

• Digestive enzymeNarrower topic: Digestive enzymes speed hydrolysis reactions while remaining available for further reactions.

• LysozymeNarrower topic: Lysozyme’s active site lowers the barrier to hydrolyzing a normally stable glycosidic bond.

• AmylaseNarrower topic: Amylase speeds starch hydrolysis without being consumed.

• NeuraminidaseNarrower topic: Neuraminidase is a catalyst that speeds sialic-acid cleavage.

• HistidineNarrower topic: Histidine’s side chain helps enzymes stabilize intermediates and transfer protons.

• ATPaseNarrower topic: ATPases lower the activation barrier for ATP hydrolysis.

• Arieh WarshelNarrower topic: Explaining how enzymes accelerate reactions is a central application of Warshel’s models.

• Frances ArnoldNarrower topic: Arnold’s work expanded the range of reactions and conditions that enzymes can catalyze.

• John CornforthNarrower topic: His work gave enzyme catalysis a precise stereochemical description.