title: Purification and Characterization of an l-Aminopeptidase from Pseudomonas putida ATCC 12633.
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.
authors.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.
authors.forename: H F
authors.initials: HF
authors.lastname: Hermes
authors.forename: T
authors.initials: T
authors.lastname: Sonke
authors.forename: P J
authors.initials: PJ
authors.lastname: Peters
authors.forename: J A
authors.initials: JA
authors.lastname: van Balken
authors.forename: J
authors.initials: J
authors.lastname: Kamphuis
authors.forename: L
authors.initials: L
authors.lastname: Dijkhuizen
authors.forename: E M
authors.initials: EM
authors.lastname: Meijer