Inhibitor binds at a site on the en

Inhibitor binds at a site on the enzyme other than the substrate binding site, altering the conformation of the enzyme molecule so that reversibly inactivate the catalytic site
A non-competitive inhibitor can combine with an enzyme molecule to produce a dead-end complex, regardless of whether a substrate molecule is bound or not.
Inhibitor must bind at a different site from the substrate.
The substrate does not affect inhibitor binding
E+I EI and ES + I ESI have an identical dissociation constant Ki (inhibitor constant)
Conversely, since non-competitive inhibitors bind to the enzyme in such a way as to reduce its catalytic properties, Vmax will be permanently reduced until the noncompetitive is removed.
However, in this case the ability of the enzyme to bind with the substrate is not affected, so that Km remains unaltered