| Autor: |
Hermes HF; 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., Sonke T, Peters PJ, van Balken JA, Kamphuis J, Dijkhuizen L, Meijer EM |
| Jazyk: |
angličtina |
| Zdroj: |
Applied and environmental microbiology [Appl Environ Microbiol] 1993 Dec; Vol. 59 (12), pp. 4330-4. |
| DOI: |
10.1128/aem.59.12.4330-4334.1993 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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