Enzymology is a branch of biochemistry that deals with the properties, activity, and significance of enzymes.

Enzymes are both proteins and biological catalysts (biocatalysts). Catalysts accelerate chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and a new field of pseudoenzyme analysis has recently grown up, recognising that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties.

Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures.

The scope of enzymology has expanded rapidly over the last century, from an early focus on the chemical and catalytic mechanisms of individual enzymes to more recent efforts to understand enzyme action in the context of dynamic, functional biological systems consisting of many interacting enzymes and proteins. Continuing progress in probing the link between molecular structure and function now promises to pave the way for a deeper understanding of the evolution and behavior of the complex biological systems that govern cellular behavior.

Enzymology research has defined and transformed our understanding of basic cellular biochemistry and has itself been transformed by emerging methods and new interactions across disciplines. The modern enzymologist uses a toolbox that includes multiple types of spectroscopy, structural biology, kinetics and molecular biology, and asks questions about enzyme function and regulation in a variety of cellular and organismal contexts.

Cooperativity, in enzymology, a phenomenon in which the shape of one subunit of an enzyme consisting of several subunits is altered by the substrate (the substance upon which an enzyme acts to form a product) or some other molecule so as to change the shape of a neighbouring subunit. The result is that the binding of a second substrate molecule to the second subunit of the enzyme differs in strength or velocity from that of the first, the third from the second, and so on. If the change in shape of the first subunit makes easier the binding of substrate to the second subunit, the effect is called positive cooperativity. In negative cooperativity, the binding of a molecule to the first subunit makes more difficult the binding of substrate to the second. See also allosteric control.

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