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Autor:
Daniela Monti, Giacomo Carrea, Maria A. Vanoni, Carlo Zambonelli, Paola Morandi, Stefano Servi, Gabriella Tedeschi, Bruno Curti, Rossana Di Lorenzo
Publikováno v:
Enzyme and microbial technology 33 (2003): 676–688.
info:cnr-pdr/source/autori:Zambonelli C., Morandi P., Vanoni M.A., Tedeschi G., Servi S., Curti B., Carrea G., Di Lorenzo R., Monti D./titolo:Cloning and expression in Escherichia coli of the gene encoding Streptomyces PMF PLD, a phospholipase D with high transphosphatydylation activity/doi:/rivista:Enzyme and microbial technology/anno:2003/pagina_da:676/pagina_a:688/intervallo_pagine:676–688/volume:33
info:cnr-pdr/source/autori:Zambonelli C., Morandi P., Vanoni M.A., Tedeschi G., Servi S., Curti B., Carrea G., Di Lorenzo R., Monti D./titolo:Cloning and expression in Escherichia coli of the gene encoding Streptomyces PMF PLD, a phospholipase D with high transphosphatydylation activity/doi:/rivista:Enzyme and microbial technology/anno:2003/pagina_da:676/pagina_a:688/intervallo_pagine:676–688/volume:33
Phospholipases D (PLDs) hydrolyze phospholipids to yield phosphatidic acid and the corresponding alcohol and catalyze a transesterification (transphosphatidylation) reaction when alcohol is present as a nucleophilic donor. Bacterial forms of PLDs hav