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- W2069656656 abstract "The gene organization and nucleotide sequence of an aspartic proteinase (AP) of plant origin were first disclosed by cDNA and genomic DNA cloning of a rice AP (oryzasin). The deduced amino acid sequence of oryzasin 1 was significantly similar to those of other APs (34–85%), with highest similarity (85%) to barley AP (HvAP). Oryzasin 1, as well as HvAP, is distinct from animal and microbial APs in that the plant APs contain a unique 104‐amino‐acid insertion in the C‐terminal region. The oryzasin 1 gene spans approximately 6.6 kbp and is composed of 14 exons and 13 introns. The exon‐intron organization of the oryzasin 1 gene is totally different from those of genes for animal and microbial APs such as human cathepsin D, rat renin, bovine chymosin, aspergillopepsin A of Aspergillus awamori , proteinase A of Saccharomyces cerevisiae and rhizopuspepsin of Rhizopus niveus , despite the fact that oryzasin 1 shows overall sequence similarity to these APs." @default.
- W2069656656 created "2016-06-24" @default.
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- W2069656656 date "1995-08-01" @default.
- W2069656656 modified "2023-10-17" @default.
- W2069656656 title "Rice Aspartic Proteinase, Oryzasin, Expressed During Seed Ripening and Germination, has a Gene Organization Distinct from Those of Animal and Microbial Aspartic Proteinases" @default.
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- W2069656656 doi "https://doi.org/10.1111/j.1432-1033.1995.tb20783.x" @default.
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