Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus

Volume: 75, Issue: 10, Pages: 625 - 633
Published: Sep 20, 2019
Abstract
Prolyl aminodipeptidase (PepX) is an enzyme that hydrolyzes peptide bonds from the N-terminus of substrates when the penultimate amino-acid residue is a proline. Prolyl peptidases are of particular interest owing to their ability to hydrolyze food allergens that contain a high percentage of proline residues. PepX from Lactobacillus helveticus was cloned and expressed in Escherichia coli as an N-terminally His-tagged recombinant construct and was...
Paper Details
Title
Structural characterization of a prolyl aminodipeptidase (PepX) from Lactobacillus helveticus
Published Date
Sep 20, 2019
Volume
75
Issue
10
Pages
625 - 633
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