Coidentity of putative amylase inhibitors from barley and finger millet with phospholipid transfer proteins inferred from amino acid sequence homology.
A class of small polypeptides, isolated from seeds of barley and millet, which had been previously identified as putative amylase inhibitors has been found to have striking amino acid sequence identity with phospholipid transfer proteins. In addition, both classes of proteins have the same molecular weight and appear to be produced by proteolytic cleavage of an amino-terminal peptide of similar size. These properties, and the lack of any known activity for the barley protein, suggest that the putative amylase inhibitors are lipid transfer proteins.
Bernhard
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DOE Plant Research Laboratory, Michigan State University, East Lansing 48824.
Somerville
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CR
D000595:Amino Acid Sequence; D000681:Amylases / Q000037:antagonists & inhibitors*; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000235:genetics*; D001467:Hordeum; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D008897:Panicum; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids / Q000378:metabolism; D010940:Plant Proteins; D012689:Sequence Homology, Nucleic Acid; D013329:Structure-Activity Relationship
D052179:Antigens, Plant; D002352:Carrier Proteins; D008565:Membrane Proteins; D049294:Phospholipid Transfer Proteins; D010743:Phospholipids; D010940:Plant Proteins; C511920:lipid transfer proteins, plant; D000681:Amylases