Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
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Proteinase k, a seryl-protease obtained from Tritirachium album, is able to specifically hydrolyze N-blocked aminoacyl transfer ribonucleic acids (tRNAs). The blocked amino acid is released, and the tRNA molecule remains able to be recharged by its cogante amino acid. Aminoacyl-tRNAs are highly resistant to hydrolysis by the protease. This activity is not due to contamination of the protease preparation. A commercial protease from Streptomyces griseus displayed a similar activity, while trypsin, chymotrypsin, and papain unspecifically hydrolyzed all charged tRNAs tested. The characteristics of the hydrolysis performed by proteinase k closely resemble the peptidyl-tRNA hydrolase activity described in different cells as a scavenger for the peptidyl-tRNA that eventually falls from the polysomes. Out results warn about a hasty identification of any N-blocked aminoacyl-tRNA hydrolase activity in the cytoplasm as an independent peptidyl-tRNA hydrolase.
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PMID:Peptidyl transfer ribonucleic acid hydrolase activity of proteinase k. 38 46