Cysteine protease

Summary

Cysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe. In fact, the latex of dozens of different plant families are known to contain cysteine proteases. Cysteine proteases are used as an ingredient in meat tenderizers. Classification The MEROPS protease classification system counts 14 superfamilies plus several currently unassigned families (as of 2013) each containing many families. Each superfamily uses the catalytic triad or dyad in a different protein fold and so represent co

Official source

https://en.wikipedia.org/wiki/Cysteine_protease

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Tuning and predicting biological affinity: aryl nitriles as cysteine protease inhibitors

Céline Freymond, Jose Enrico Quijano Quinsaat, Pablo Rivera Fuentes

A series of aryl nitrile-based ligands were prepd. to investigate the effect of their electrophilicity on the affinity against the cysteine proteases rhodesain and human cathepsin L. D. functional theory calcns. provided relative reactivities of the nitriles, enabling prediction of their biol. affinity and cytotoxicity and a clear structure-activity relationship.

2012

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Motivated by the recent implication of cysteine protease cathepsin L as a potential target for anti-cancer drug development, we used a conditional MycER(TAM); Bcl-x(L) model of pancreatic neuroendocrine tumorigenesis (PNET) to assess the role of cathepsin L in Myc-induced tumor progression. By employing a cysteine cathepsin activity probe in vivo and in vitro, we first established that cathepsin activity increases during the initial stages of MycER(TAM); Bcl-x(L) tumor development. Among the cathepsin family members investigated, only cathepsin L was predominately produced by beta-tumor cells in neoplastic pancreata and, consistent with this, cathepsin L mRNA expression was rapidly upregulated following Myc activation in the beta cell compartment. By contrast, cathepsins B, S and C were highly enriched in tumor-infiltrating leukocytes. Genetic deletion of cathepsin L had no discernible effect on the initiation of neoplastic growth or concordant angiogenesis. However, the tumors that developed in the cathepsin L-deficient background were markedly reduced in size relative to their typical wild-type counterparts, indicative of a role for cathepsin L in enabling expansive tumor growth. Thus, genetic blockade of cathepsin L activity is inferred to retard Myc-driven tumor growth, encouraging the potential utility of pharmacological inhibitors of cysteine cathepsins in treating late stage tumors.

Public Library of Science2015

Evolution of S-Cysteinylated and S-Glutathionylated Thiol Precursors during Oxidation of Melon B. and Sauvignon blanc Musts

Jérôme Vialaret

Thiol precursor content in Melon B. and Sauvignon blanc grape juices obtained under vacuum was determined by quantifying cysteinylated and glutathionylated conjugates of 3-mercaptohexan-1-ol (3MH) and 4-methyl-4-mercaptopentan-2-one (4MMP). This characterization allowed the study of thiol precursor evolution during ripening of Sauvignon blanc grapes in several viticultural situations together with grape reaction product (GRP) and the main substrate of polyphenoloxidase, that is, caftaric acid. Concentration of precursors greatly increased during ripening except for the cysteinylated conjugate of 4MMP. Precursor evolution was also monitored during the oxidation of grape juice. Addition of oxygen to a grape juice set off the enzymatic oxidation of hydroxycinnamic acids but did not negatively affect precursor concentrations. Part of the glutathionylated precursor of the 3MH was produced during prefermentative operations (up to 140% in Sauvignon blanc). Consequently, this precursor naturally occurring in grapes was also formed during prefermentative operations. The proportion of biogenetic and prefermentary formation of the glutathionylated precursor of 3MH was different under industrial conditions depending on the grape variety considered. Addition of glutathione and hexenal in grape juices of Melon B. and Sauvignon induced an increase of the production of 3MH and consequently of its acetate in the resulting wines. Residual glutathione in must has to be preserved to enhance the aromatic potential of grapes.

2010