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The First Example of an RNA Urea Synthase: Selection through the Enzyme Active Site of Human Neutrophile Elastase
Author(s) -
Nieuwlandt Dan,
West Madeline,
Cheng Xiaoqin,
Kirshenheuter Gary,
Eaton Bruce E.
Publication year - 2003
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300610
Subject(s) - tripeptide , rna , biochemistry , enzyme , elastase , chemistry , serine protease , proteases , phosphonate , protease , urea , stereochemistry , gene , peptide
RNA catalysts : In vitro selection from a random library of RNA sequences gave RNA urea synthases able to utilize tripeptides as substrates (see scheme; HNE, human neutrophile elastase). The tripeptide substrates were mechanism‐based protease suicide substrates. Stereoselection of serine protease tripeptide phosphonate inhibitors was achieved by RNA catalysis. The RNA urea synthases showed a high degree of diastereoselectivity for the most potent protease suicide inhibitor.