Plant Physiology 99:1179-1183 (1992)
© 1992 American Society of Plant Biologists
Metabolism and Enzymology
Sequencing and Characterization of the Soybean Leaf Metalloproteinase 1
Structural and Functional Similarity to the Matrix Metalloproteinase Family
Gerard McGeehan,
William Burkhart,
Robert Anderegg,
J. David Becherer,
Jeffery W. Gillikin and
John S. Graham
Department of Biochemistry, Glaxo Research Institute, Research Triangle Park, North Carolina 27709,
Department of Structural and Biophysical Chemistry, Glaxo Research Institute, Research Triangle Park, North Carolina 27709,
Department of Biological Sciences, Bowling Green State University, Bowling Green, Ohio 43403
A novel zinc endoproteinase has been sequenced and characterized from soybean leaves (Glycine max var Williams 82) and has been designated as Protein Identification Resource accession No. A41820 SMEP1 (soybean metalloendoproteinase 1). Comparison of the primary amino acid sequence with other zinc proteinases revealed the enzyme to be a new member of the matrix metalloproteinase (MMP) family of enzymes. SMEP was found to have MMP cleavage specificity toward peptide substrates and the enzyme is specifically inhibited by naturally occurring tissue inhibitors of MMPs through a high-affinity interaction (inhibitor concentration resulting in an approximate 50% decrease in enzyme activity = 23 x 10–9 molar). Together, these results suggest that the origin of the MMP family of enzymes and their cognate inhibitors predates the divergence of plants and animals.
1 Supported by Glaxo Research Laboratories and the Ohio Board of Regents.
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