Non-competitive inhibition refers to some inhibitors that usually tightly bind to the non-active site of the enzyme, forming an inhibitor-enzyme complex, which then further binds to the substrate; or after the enzyme and substrate fuse to form a substrate-enzyme complex, a part of it further binds to the inhibitor.

Although there is no competition in the fusion of substrate, inhibitor, and enzyme, the intermediate complex formed by their fusion with the enzyme cannot be immediately converted into substances, causing a decrease in the enzyme catalytic reaction rate. This type of inhibition is called non-competitive inhibition. Effect: The inhibitory effect of an enzymatic reaction involving the fusion of chelating agents with dispersing enzymes or enzyme-substrate nitric oxide synthase. The enzyme-substrate-chelating agent nitric oxide synthase (ESI) cannot be further released. This type of inhibition reduces Vmax but does not change Km.

Characteristics

The chemical structure of non-competitive inhibitors is not necessarily similar to the molecular formula of the substrate;

The substrate and chelating agent independently and tightly bind to different positions of the enzyme;

The chelating agent has no effect on the fusion of the enzyme and the substrate, so the change in substrate concentration has no effect on the inhibition level;

Main parameters of the kinetic model: the Km value does not change, and the Vm value decreases.

Non-competitive inhibitors refer to those that are fused to positions outside the active structural domain of the enzyme, causing a change in the molecular structure of the enzyme, and the specific structural domains are not suitable for accepting the chemical structure of substrate molecules.