Microbial Relatives of Seed Storage Proteins: Conservation of Motifs in a Functionally Diverse Superfamily of Enzymes |
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Authors: | Jim M. Dunwell Paul J. Gane |
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Affiliation: | (1) Department of Agricultural Botany, School of Plant Sciences, The University of Reading, Whiteknights, PO Box 221, Reading RG6 6AS, United Kingdom, GB;(2) Institute of Food Research, Reading Laboratory, Earley Gate, Whiteknights Road, Reading RG6 6BZ, United Kingdom, GB |
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Abstract: | Plant storage proteins comprise a major part of the human diet. Sequence analysis has revealed that these proteins probably share a common ancestor with a fungal oxalate decarboxylase and/or related bacterial genes. Additionally, all these proteins share a central core sequence with several other functionally diverse enzymes and binding proteins, many of which are associated with synthesis of the extracellular matrix during sporulation/encystment. A possible prokaryotic relative of this sequence is a bacterial protein (SASP) known to bind to DNA and thereby protect spores from extreme environmental conditions. This ability to maintain cell viability during periods of dehydration in spores and seeds may relate to absolute conservation of residues involved in structure determination. Received: 25 April 1997 / Accepted: 29 July 1997 |
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Keywords: | : Seed storage proteins — Enzyme superfamily — Protein domain — Germin — Oxalate oxidase — Histidine cluster — Mannose metabolism |
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