Related Experiment Video
Updated: Aug 14, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Purification and Characterization of an l-Aminopeptidase from Pseudomonas putida ATCC 12633
H F Hermes1, T Sonke, P J Peters
1DSM Research, Bio-organic Chemistry section, P.O. Box 18, 6160 MD Geleen, and Department of Microbiology, University of Groningen, Kerklaan 30, 9571 NN Haren, The Netherlands.
Abstract:
An l-aminopeptidase of Pseudomonas putida, used in an industrial process for the hydrolysis of d,l-amino acid amide racemates, was purified to homogeneity. The highly l-enantioselective enzyme resembled thiol reagent-sensitive alkaline serine proteinases and was strongly activated by divalent cations. It possessed a high substrate specificity for dipeptides and alpha-H amino acid amides, e.g., l-phenylglycine amide.
