Abstract
The nucleotide sequence and derived amino acid sequence of two different β-glucosidase cDNA clones were determined. One clone (TRE104) was identified as the cyanogenic β-glucosidase by homology with the N-terminal and internal peptide amino acid sequence of the purified enzyme. The biological function of the other β-glycosidase (TRE361) is not known. Co-segregation of genomic restriction fragments uniquely identified by each cDNA clone shows that these two genes are linked in the white clover genome. Both TRE104 and TRE361 fragments co-segregate with cyanogenic β-glucosidase activity. Extensive homology was found between the white clover β-glucosidase sequences and a group of prokaryote and mammalian β-glycosidases. This group of sequences has no homology with a separate set of β-glucosidase genes isolated from fungi and the thermophilic bacterium Clostridium thermocellum.
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Oxtoby, E., Dunn, M.A., Pancoro, A. et al. Nucleotide and derived amino acid sequence of the cyanogenic β-glucosidase (linamarase) from white clover (Trifolium repens L.). Plant Mol Biol 17, 209–219 (1991). https://doi.org/10.1007/BF00039495
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DOI: https://doi.org/10.1007/BF00039495