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. 1993 Dec;59(12):4330–4334. doi: 10.1128/aem.59.12.4330-4334.1993

Purification and Characterization of an l-Aminopeptidase from Pseudomonas putida ATCC 12633

H F M Hermes 1, T Sonke 1, P J H Peters 1, J A M van Balken 1, J Kamphuis 1, L Dijkhuizen 1,*, E M Meijer 1
PMCID: PMC195905  PMID: 16349130

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 α-H amino acid amides, e.g., l-phenylglycine amide.

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Selected References

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