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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Blotting, Northern
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Cardenolides / metabolism
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Cloning, Molecular
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DNA, Complementary / chemistry
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DNA, Complementary / genetics*
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Digitalis / enzymology
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Digitalis / genetics*
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Escherichia coli / genetics*
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Gene Expression Regulation, Enzymologic
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Glucosidases / genetics*
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Glucosidases / metabolism
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Molecular Sequence Data
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Plant Proteins*
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Plants, Medicinal*
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Plants, Toxic*
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Sequence Alignment
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Sequence Analysis, DNA
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Sequence Homology, Amino Acid
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Tissue Distribution
Substances
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Cardenolides
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DNA, Complementary
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Plant Proteins
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RNA, Messenger
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Cardenolide 16-O-glucohydrolase, Digitalis lanata
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Glucosidases