Asparagine Peptide Lyases: a Seventh Catalytic Type of Proteolytic Enzymes

Overview

Journal J Biol Chem

Specialty Biochemistry

Date 2011 Aug 12

PMID 21832066

Citations 33

Authors

Neil David Rawlings

Alan John Barrett

Alex Bateman

Affiliations

Soon will be listed here.

Abstract

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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