The transformation product of lactacystin clasto-lactacystin β-lactone (also known as omuralide) covalently modifies the amino-terminal threonine of specific catalytic subunits of the proteasome, a discovery that helped to establish the proteasome as a mechanistically novel class of protease: an amino-terminal threonine protease. The molecule is commonly used in biochemistry and cell biology laboratories as a selective inhibitor of the proteasome. The first total synthesis of lactacystin was developed in 1992 by Corey and Reichard, and a number of other syntheses of this molecule have also been published.
The transformed form of lactacystin, clasto-lactacystin β-lactone (also known as omuralide), covalently modifies the amino-terminal threonine of specific catalytic subunits of the proteasome. This discovery helped to classify the proteasome as a novel class of protease: an amino-terminal threonine protease. The molecule is frequently used in biochemistry and cell biology laboratories as a selective inhibitor of the proteasome. The initial total synthesis of lactacystin was developed by Corey and Reichard in 1992, and several other syntheses of this compound have been published.