PMID:20350528

Citation	Bhosale, M, Pande, S, Kumar, A, Kairamkonda, S and Nandi, D (2010) Characterization of two M17 family members in Escherichia coli, Peptidase A and Peptidase B. Biochem. Biophys. Res. Commun. 395:76-81
Abstract	Escherichia coli encodes two aminopeptidases belonging to the M17 family: Peptidase A (PepA) and Peptidase B (PepB). To gain insights into their substrate specificities, PepA or PepB were overexpressed in Delta pepN, which shows greatly reduced activity against the majority of amino acid substrates. Overexpression of PepA or PepB increases catalytic activity of several aminopeptidase substrates and partially rescues growth of Delta pepN during nutritional downshift and high temperature stress. Purified PepA and PepB display broad substrate specificity and Leu, Lys, Met and Gly are preferred substrates. However, distinct differences are observed between these two paralogs: PepA is more stable at high temperature whereas PepB displays broader substrate specificity as it cleaves Asp and insulin B chain peptide. Importantly, this strategy, i.e. overexpression of peptidases in Delta pepN and screening a panel of substrates for cleavage, can be used to rapidly identify peptidases with novel substrate specificities encoded in genomes of different organisms.
Links	PubMed Online version:10.1016/j.bbrc.2010.03.142
Keywords	Aminopeptidases/antagonists & inhibitors; Aminopeptidases/chemistry; Aminopeptidases/isolation & purification; Bacterial Proteins/antagonists & inhibitors; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/antagonists & inhibitors; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/chemistry; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/isolation & purification; Enzyme Stability; Escherichia coli/enzymology; Escherichia coli Proteins/antagonists & inhibitors; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Hydrolysis; Substrate Specificity
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