Please use this identifier to cite or link to this item:
Title: Structure and function of plant aspartic proteinases
Authors: Simões, Isaura 
Faro, Carlos 
Issue Date: 2004
Citation: European Journal of Biochemistry. 271:11 (2004) 2067-2075
Abstract: Aspartic proteinases of the A1 family are widely distributed among plant species and have been purified from a variety of tissues. They are most active at acidic pH, are specifically inhibited by pepstatin A and contain two aspartic residues indispensible for catalytic activity. The three-dimensional structure of two plant aspartic proteinases has been determined, sharing significant structural similarity with other known structures of mammalian aspartic proteinases. With a few exceptions, the majority of plant aspartic proteinases identified so far are synthesized with a prepro-domain and subsequently converted to mature two-chain enzymes. A characteristic feature of the majority of plant aspartic proteinase precursors is the presence of an extra protein domain of about 100 amino acids known as the plant-specific insert, which is highly similar both in sequence and structure to saposin-like proteins. This insert is usually removed during processing and is absent from the mature form of the enzyme. Its functions are still unclear but a role in the vacuolar targeting of the precursors has been proposed. The biological role of plant aspartic proteinases is also not completely established. Nevertheless, their involvement in protein processing or degradation under different conditions and in different stages of plant development suggests some functional specialization. Based on the recent findings on the diversity of A1 family members in Arabidopsis thaliana, new questions concerning novel structure2013function relationships among plant aspartic proteinases are now starting to be addressed.
DOI: 10.1111/j.1432-1033.2004.04136.x
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

Files in This Item:
File Description SizeFormat
obra.pdf282.59 kBAdobe PDFView/Open
Show full item record


checked on Nov 11, 2022

Citations 1

checked on May 2, 2023

Page view(s)

checked on Apr 9, 2024


checked on Apr 9, 2024

Google ScholarTM




Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.