PROTEINASE-CATALYZED TRANSAMIDATION AND ITS EFFICIENCY
نویسندگان
چکیده
منابع مشابه
Specificity of papain-catalyzed transamidation reactions.
In the experiments reported in the present communication, these studies have been extended with special reference to the specificity of the enzyme toward the dipeptide used as replacement agent. It had been suggested (1) that the value of pKz’ of a dipeptide is a determining factor in the efficiency with which it can participate in a transamidation reaction at ‘a given pH. This suggestion has b...
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Previous publications from this laboratory (l-3) have described the catalysis of transamidation reactions by the proteinases papain, ficin, and crystalline chymotrypsin. In addition, preliminary experiments were reported on replacement reactions catalyzed by beef spleen cathepsin C, an intracellular endopeptidase of animal tissues, which resembles pancreatic chymotrypsin in its specificity. The...
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Transamidation, or the conversion of one amide to another, is a long-standing challenge in organic synthesis. Although notable progress has been made in the transamidation of primary amides, the transamidation of secondary amides has remained underdeveloped, especially when considering aliphatic substrates. Herein, we report a two-step approach to achieve the transamidation of secondary aliphat...
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Zirconocene dichloride (Cp(2)ZrCl(2)) has been shown to be an effective catalyst for the transamidation of primary amides with amines in cyclohexane at 80 °C in 5-24 hours. For favourable substrates, the reaction can be performed at temperatures as low as 30 °C.
متن کاملSelenopeptide Transamidation and Metathesis
Selenopeptides can be transamidated by cysteinyl peptides in water using mild conditions (pH 5.5, 37 °C) in the presence of an arylthiol catalyst. Similar conditions also catalyze the metathesis of selenopeptides. The usefulness of the selenophosphine derived from TCEP (TCEP═Se) for inhibiting the TCEP-induced deselenization of selenocysteine residue is also reported.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1954
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)65667-4