Department of Biochemistry, Glaxo Research Institute, Research Triangle Park, North Carolina 27709.
Plant Physiol. 1992 Jul;99(3):1179-83. doi: 10.1104/pp.99.3.1179.
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.
一种新型锌内肽酶已从大豆叶片（Glycine max var Williams 82）中被测序并鉴定，被指定为蛋白质鉴定资源编号 A41820 SMEP1（大豆金属内肽酶 1）。与其他锌蛋白酶的一级氨基酸序列比较表明，该酶是基质金属蛋白酶（MMP）家族酶的一个新成员。SMEP 对肽底物具有 MMP 切割特异性，并且该酶通过高亲和力相互作用（抑制剂浓度导致酶活性降低约 50%时的浓度=23 x 10(-9)摩尔）被天然存在的 MMP 组织抑制剂特异性抑制。这些结果表明，MMP 酶家族及其同源抑制剂的起源早于植物和动物的分化。
