Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D

Simon A. Cater , Wendy E. Lees , Jeffrey Hill , Joze Brzin , John Kay , Lowri H. Phylip
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引用次数: 28

Abstract

The interaction of a variety of aspartic proteinases with a recombinant tomato protein produced in Pichia pastoris was investigated. Only human cathepsin D and, even more potently, proteinase A from Saccharomyces cerevisiae were inhibited. The tomato polypeptide has >80% sequence identity to a previously reported potato inhibitor of cathepsin D. Re-evaluation of the potato inhibitor revealed that it too was more potent (>20-fold) towards yeast proteinase A than cathepsin D and so might be renamed the potato inhibitor of proteinase A. The potency towards yeast proteinase A may reflect a similarity between this fungal enzyme and aspartic proteinases produced by fungal pathogens which attack tomato and/or potatoes.

从番茄和马铃薯中提取的天冬氨酸蛋白酶抑制剂对酵母蛋白酶A比组织蛋白酶D更有效
研究了多种天冬氨酸蛋白酶与毕赤酵母生产的重组番茄蛋白的相互作用。只有人组织蛋白酶D和更有效的酿酒酵母蛋白酶A被抑制。该番茄多肽与先前报道的马铃薯组织蛋白酶D抑制剂具有80%的序列同源性。对马铃薯抑制剂的重新评价表明,该马铃薯抑制剂对酵母蛋白酶a的效力也比组织蛋白酶D强(20倍),因此可能被重新命名为马铃薯蛋白酶a抑制剂。对酵母蛋白酶a的效力可能反映了该真菌酶与侵袭番茄和/或马铃薯的真菌病原体产生的天冬氨酸蛋白酶的相似性。
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