Olczak M, Kobiałka M, Watorek W
Institute of Biochemistry and Molecular Biology, Wroclaw University, Tamka 2, 50-137, Wroclaw, Poland.
Biochim Biophys Acta. 2000 May 23;1478(2):239-47. doi: 10.1016/s0167-4838(00)00024-8.
A phosphatase cleaving the pyrophosphate bond in diphosphonucleotides and phosphodiester bond in various phosphodiesters (pH optimum at 6.25) was purified from yellow lupin (Lupinus luteus L.) seeds. The enzyme is 75 kDa monomeric glycoprotein (pI=6.4) with 4.4% of carbohydrate (mannose, N-acetylglucosamine, fucose and xylose). Analysis of its partial amino acid sequence (8 peptides, 101 amino acid residues) together with no divalent cation requirements for catalysis points out that the purified enzyme is different from known plant pyrophosphate cleaving enzymes (apyrases and inorganic pyrophosphatases). Its physiological role could be related to a regulation of diphosphonucleotides level in plant metabolism.
从黄羽扇豆（Lupinus luteus L.）种子中纯化出一种磷酸酶，该酶可裂解二磷酸核苷酸中的焦磷酸键以及各种磷酸二酯中的磷酸二酯键（最适pH为6.25）。该酶是一种75 kDa的单体糖蛋白（pI = 6.4），碳水化合物含量为4.4%（包括甘露糖、N-乙酰葡糖胺、岩藻糖和木糖）。对其部分氨基酸序列（8个肽段，101个氨基酸残基）的分析以及催化过程中对二价阳离子无需求表明，纯化得到的这种酶不同于已知的植物焦磷酸裂解酶（焦磷酸酶和无机焦磷酸酶）。其生理作用可能与植物代谢中二磷酸核苷酸水平的调节有关。
