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Structure and Possible Function of Aspartic Proteinases in Barley and other Plants

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Aspartic Proteinases

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 362))

Abstract

The aim of this short article is to review the literature on plant aspartic proteinases in general as well as to present more detailed information on our studies on the barley aspartic proteinase. Aspartic proteinases (EC 3.4.23) are widely dispersed in the plant kingdom including monocotyledonous and dicotyledonous species as well as gymnosperms. These enzymes have been detected in seeds, leaves and flowers in different plants as well as in the digestive fluid of some insectivorous species. Like their animal and microbial counterparts (1–3), plant aspartic proteinases are inhibited by pepstatin and preferentially cleave peptide bonds between amino acid residues with large hydrophobic side chains. The biological functions of plant aspartic proteinases are not as well characterized as those of animal aspartic proteinases. In the insectivorous plant Nepenthes, aspartic proteinase may participate in the digestion of insects trapped in the digestive fluid of the pitcher. In the leaves of tomato and tobacco, aspartic proteinases may contribute to the hydrolysis of extracellular pathogenesis-related proteins. Aspartic proteinases have also been reported to be associated with the intracellular storage protein bodies of hemp and buckwheat seeds and to take part in the hydrolysis of storage proteins in wheat and cocoa in vitro. In addition, aspartic proteinases from seeds have been shown to process the Arabidopsis 2S albumin storage proteins in vitro. The cDNA-derived primary structures of barley, rice, and cardoon aspartic proteinases are known. The open reading frame of the barley enzyme consists of a 66-amino acid preprosequence and a 442 residues long mature protein, about the same size as recently also revealed for rice and cardoon enzymes.

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Authors and Affiliations

  1. Institute of Biotechnology, University of Helsinki, P.O. Box 45, FIN-00014, Finland

    Jukka Kervinen, Kirsi Törmäkangas, Pia Runeberg-Roos & Teemu H. Teeri

  2. Department of Crystallography Birkbeck College, University of London, Malet Street, London, WCIE 7HX, UK

    Kunchur Guruprasad & Tom Blundell

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  1. Jukka Kervinen
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  2. Kirsi Törmäkangas
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  3. Pia Runeberg-Roos
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  4. Kunchur Guruprasad
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  6. Teemu H. Teeri
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  1. The University of Tokyo, Tokyo, Japan

    Kenji Takahashi

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Kervinen, J., Törmäkangas, K., Runeberg-Roos, P., Guruprasad, K., Blundell, T., Teeri, T.H. (1995). Structure and Possible Function of Aspartic Proteinases in Barley and other Plants. In: Takahashi, K. (eds) Aspartic Proteinases. Advances in Experimental Medicine and Biology, vol 362. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1871-6_28

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  • DOI: https://doi.org/10.1007/978-1-4615-1871-6_28

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