Purification and Characterization of an l-Aminopeptidase from Pseudomonas putida ATCC 12633 |
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| Authors: | Hermes H F Sonke T Peters P J van Balken J A Kamphuis J Dijkhuizen L Meijer E M |
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| Affiliation: | DSM 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. |
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| 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. |
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