title: Aspartic proteinase inhibitors from tomato and potato are more potent against yeast proteinase A than cathepsin D.
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.
authors: School of Biosciences, Cardiff University, P.O. Box 911, Cardiff CF10 3US, UK.
authors: Simon A
authors: SA
authors: Cater
authors: Wendy E
authors: WE
authors: Lees
authors: Jeffrey
authors: J
authors: Hill
authors: Joze
authors: J
authors: Brzin
authors: John
authors: J
authors: Kay
authors: Lowri H
authors: LH
authors: Phylip
mesh_terms: D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D002402:Cathepsin D / Q000037:antagonists & inhibitors* / Q000737:chemistry; D003001:Cloning, Molecular; D004791:Enzyme Inhibitors / Q000494:pharmacology; D018551:Solanum lycopersicum / Q000235:genetics; D008969:Molecular Sequence Data; D010843:Pichia / Q000235:genetics / Q000378:metabolism; D010957:Plasmids; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D011198:Solanum tuberosum / Q000235:genetics
chemical_list: D004791:Enzyme Inhibitors; D016282:Aspartic Acid Endopeptidases; C022442:aspergillopepsin II; D002402:Cathepsin D