Enzymes catalyze chemical reactions involving the substrate (s). The substrate is transformed into one or more products, which are then released from the active site.

This articles reviews positive and negative cooperativity in enzymes and how this is expressed numerically by the Hill coefficient.

This article discusses the specific effects of various enzyme inhibitors on kinetic graphs, highlighting how these visual tools can be used to pinpoint the type of inhibition involved.

Learn how enzymes speed up reactions, the uniqueness of their active sites, and the transformations during substrate binding. Discover the crucial roles of active and allosteric sites in enzyme regulation.

The various types of inhibitors are distinguished by whether they bind only to the free enzyme, only to the enzyme-substrate complex, or to both the enzyme and the enzyme-substrate complex (as well as …

Explore how enzymes speed up reactions, the role of substrate concentrations, and the importance of the Michaelis constant. Discover how to score an enzyme's catalytic efficiency using Kcat and KM.

These molecules are the enzyme's substrates. The part of the enzyme where the substrate binds is called the active site. The enzyme holds the substrate in a specific way (called the enzyme/substrate …

The part of the enzyme where the substrate binds is called the active site. Here, the enzyme changes shape slightly, fitting tightly with the substrate and forming the enzyme/substrate complex.

The various types of inhibitors are distinguished by whether they bind only to the free enzyme, only to the enzyme-substrate complex, or to both the enzyme and the enzyme-substrate complex (as well as …

An enzyme is just a special chemical. This means that it can react and form temporary bonds. The same way sodium and chlorine come together, enzymes and their substrates can come together. Hope this …