Enzyme Research

New enzyme research study findings have been reported from K. Schilling et al

Published in Drug Law Weekly, March 24th, 2009

Research findings, 'Selectivity of propeptide-enzyme interaction in cathepsin L-like cysteine proteases,' are discussed in a new report. According to a study from Jena, Germany, "Cathepsin L-like endopeptidases of the papain family are synthesized as proenzymes. N-terminal proregions are essential for folding and latency of the enzyme unit."

"While selectivity has been reported for the inhibitory function of papain-family propeptides, there is no systematic investigation of the selectivity of their chaperone-like function to date. The chaperone-like cross-reactivity between the cathepsins S, K, and L were thoroughly quantified in trans-experiments, i.e., with isolated...

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Source: Drug Law Weekly (2009-03-24)

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