Leupeptin

Leupeptin, also known as N-acetyl-L-leucyl-L-leucyl-L-argininal, is a naturally occurring protease inhibitor that can inhibit cysteine, serine and threonine peptidases.

These proteases, if freely present in the lysate, would destroy any products from the reaction being studied, and make the experiment uninterpretable.

Leupeptin is an organic compound produced by actinomycetes, which inhibits serine, cysteine and threonine proteases.

Leupeptin is a competitive transition state inhibitor and its inhibition may be relieved by an excess of substrate.

Leupeptin is soluble in water (stable for 1 week at 4 °C and 1 month at −20 °C), ethanol, acetic acid and DMF.

Stereo, skeletal formula of leupeptin
Stereo, skeletal formula of leupeptin
Crystal structure of Leupeptin (silver) in the Trypsin (green) binding pocket.
Crystal structure of Leupeptin (silver) in the Trypsin (green) binding pocket. Hydrogen bonds are shown as yellow dotted lines. Rendered from PDB 1JRS .