Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 2011-11, Vol.286 (44), p.38321-38328
Main Authors: Rawlings, Neil David, Barrett, Alan John, Bateman, Alex
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Asparagine - chemistry
Biological Transport
Catalysis
Computational Biology
Escherichia coli - enzymology
Lyases - chemistry
Models, Molecular
Multigene Family
Peptide Hydrolases - chemistry
Peptide Hydrolases - classification
Peptides - chemistry
Protein Conformation
Protein Processing, Post-Translational
Protein Structure, Tertiary
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M111.260026