Abstract
Protein inhibitors of enzymes, which have potentially deleterious effects in animal nutrition and possible defensive functions against insect and microbial pests, are of widespread occurrence in plants1,2. Because cereals provide about 55% of direct human protein intake their inhibitors have received much attention3. The amino-acid sequences of α-amylase inhibitors in wheat4–6, and ragi (Eleusine coracana)7; proteinase inhibitors from maize8 and barley9,10; and bifunctional proteinase/amylase inhibitors in ragi11, barley12,13 and wheat14 show varied evolutionary relationships. Here we describe the sequence of a maize protein which is a potent in vitro inhibitor of bovine trypsin and the α-amylase from Tribolium castaneum beetles. The protein has little similarity to any of the other enzyme inhibitors, but is highly similar to the intensely sweet protein thaumatin15 and to a protein induced in tobacco following infection by tobacco mosaic virus (TMV)16. This unexpected finding suggests a possible function for these proteins.
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Richardson, M., Valdes-Rodriguez, S. & Blanco-Labra, A. A possible function for thaumatin and a TMV-induced protein suggested by homology to a maize inhibitor. Nature 327, 432–434 (1987). https://doi.org/10.1038/327432a0
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DOI: https://doi.org/10.1038/327432a0
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