Cloning and functional expression in Escherichia coli of a cDNA encoding cardenolide 16'-O-glucohydrolase from Digitalis lanata Ehrh |
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Authors: | Framm J J Peterson A Thoeringer C Pangert A Hornung E Feussner I Luckner M Lindemann P |
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Affiliation: | Institut für Pharmazeutische Biologie, Martin-Luther-Universit?t, Hoher Weg 8, D-06120 Halle (Saale), Germany. |
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Abstract: | A clone of cardenolide 16'-O-glucohydrolase cDNA (CGH I) was obtained from Digitalis lanata which encodes a protein of 642 amino acids (calculated molecular mass 73.2 kDa). The amino acid sequence derived from CGH I showed high homology to a widely distributed family of beta-glucohydrolases (glycosyl hydrolases family 1). The recombinant CGH I protein produced in Escherichia coli had CGH I activity. CGH I mRNA was detected in leaves, flowers, stems and fruits of D. lanata. |
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