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

被引：25

作者：

Cater, SA

Lees, WE

Hill, J

Brzin, J

Kay, J

Phylip, LH

机构：

[1] Univ Wales Coll Cardiff, Sch Biosci, Cardiff CF10 3US, S Glam, Wales

[2] Jozef Stefan Inst, SI-1000 Ljubljana, Slovenia

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1596卷 / 01期

基金：

英国生物技术与生命科学研究理事会;

关键词：

protein inhibitor; aspartic proteinase; inhibition of yeast proteinase A; inhibition of cathepsin D; tomato inhibitor; potato inhibitor;

D O I：

10.1016/S0167-4838(02)00206-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. Reevaluation 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. (C) 2002 Elsevier Science B.V. M rights reserved.

引用

页码：76 / 82

页数：7

共 23 条

[1] Purification, characterization and cloning of an aspartic proteinase inhibitor from squash phloem exudate [J].