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enzymes. Papain, the archetype member of this family has industrial and pharmaceutical applications. The papain-family cysteine proteases share a typical overall fold, comprising two domains, with the active site located in a cleft at their interface. Their enzymatic activity is related to a catalytic dyad formed by a Cys(-) and His(+). Despite the similarities, variations in properties like substrate specificity, activity and thermal stability have been observed in some of these proteases. Three such proteases, Ervatamins A, B and C, have been isolated from the latex of a tropical plant Ervatamia coronaria and characterized. Structural and biochemical studies on these proteases have helped us to identify a few amino acid residues which may be thought to be responsible for substantial changes in their functional properties. This structure-based knowledge is being utilized to design proteases for improved industrial applications.

Mechanism of stereospecific substrate recognition by LL-diaminopimelate aminotransferase