enzymologie

Enzymologie, or enzymology, is the branch of biochemistry that studies enzymes—biological catalysts that accelerate chemical reactions in living organisms. Most enzymes are proteins, though ribozymes, RNA molecules with catalytic activity, also exist. Enzymes work by binding substrates at an active site, often employing induced fit to stabilize the transition state. Specificity is a hallmark: many enzymes act on a single substrate or a small set of related substrates. Historically, the concept of enzymes emerged in the 19th century with Payen and Persoz's discovery of diastase in 1833.

Enzymes operate under defined conditions of temperature, pH, and ionic strength, and can require cofactors such as metal ions or organic molecules (coenzymes like NAD+, FAD). The rate of an enzymatic reaction is described by Michaelis-Menten kinetics, with parameters such as Km and Vmax; kcat measures turnover. Enzyme activity is regulated by inhibitors, activators, and allosteric effectors, enabling control of metabolic flux.

Enzymes are classified into six major classes according to the reactions they catalyze: oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases, with activity organized in the Enzyme Commission (EC) numbering system. Purification and characterization rely on chromatography, electrophoresis, and spectroscopic assays.

Applications of enzymology include medical diagnostics (enzyme activity markers in blood), industrial biocatalysis (synthesis and modification of chemicals), and biotechnology, where recombinant enzymes enable new therapies and sustainable processes. Ongoing research combines structural biology, kinetics, and computational methods to understand mechanisms and to engineer enzymes with altered specificity, stability, or activity.