| Literature DB >> 16349130 |
H F Hermes1, T Sonke, P J Peters, J A van Balken, J Kamphuis, L Dijkhuizen, E M Meijer.
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.Entities:
Year: 1993 PMID: 16349130 PMCID: PMC195905 DOI: 10.1128/aem.59.12.4330-4334.1993
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792