Structure and function of plant aspartic proteinases

Simões I, Faro C ...see all

European Journal of Biochemistry, vol. 271, issue 11 (2004) pp. 2067-2075

  • 138


    Mendeley users who have this article in their library.
  • 141


    Citations of this article.
Sign in to save reference


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 structure-function relationships among plant aspartic proteinases are now starting to be addressed.

Author-supplied keywords

  • Aspartic proteinases
  • Cardosin
  • Phytepsin
  • Programmed cell death
  • Stress response

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Get full text


  • Isaura Simões

  • Carlos Faro

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free