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Asparagine Peptide Lyases
N. Rawlings, A. Barrett, A. Bateman
Published 2011 · Chemistry, Medicine
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Background: Proteolytic enzymes perform post-translational, processing and digestion of proteins and peptides. Six catalytic types have already been recognized, all of them peptidases cleaving substrates by hydrolysis. Results: A seventh catalytic type has now been identified and ten families have been assembled. Conclusion: The newly identified enzymes are not hydrolases but lyases utilizing asparagine as a nucleophile. Significance: Not all proteolytic enzymes are peptidases. The terms “proteolytic enzyme” and “peptidase” have been treated as synonymous, and all proteolytic enzymes have been considered to be hydrolases (EC 3.4). However, the recent discovery of proteins that cleave themselves at asparagine residues indicates that not all peptide bond cleavage occurs by hydrolysis. These self-cleaving proteins include the Tsh protein precursor of Escherichia coli, in which the large C-terminal propeptide acts as an autotransporter; certain viral coat proteins; and proteins containing inteins. Proteolysis is the action of an amidine lyase (EC 4.3.2). These proteolytic enzymes are also the first in which the nucleophile is an asparagine, defining the seventh proteolytic catalytic type and the first to be discovered since 2004. We have assembled ten families based on sequence similarity in which cleavage is thought to be catalyzed by an asparagine.
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