论文部分内容阅读
从水稻叶片部分纯化了水解磷酸烯醇式丙酮酸的磷酸酯酶，其Ｋｍ（ＰＥＰ）为０．１ｍｍｏｌ／Ｌ，最适ＰＨ５．３．在偏酸性ＰＨ条件下（ＰＨ４．０～７．２）稳定，对热亦较稳定．酶活性受Ｐｉ强烈抑制．它对其底物要求不专一，能水解多种含磷酯键的化合物．表明它是一种非专一性的酸性磷酸酯酶。各种含磷酯键的代谢物对酶活性起竞争性抑制作用，且表现出叠加性．Ｃｕ（２＋）、Ｚｎ（２＋）和Ｆｅ（２＋）抑制酶活性，Ｍｇ（２＋）、Ｍｎ（２＋）、Ｃａ（２＋）、Ｃｏ（２＋）和ＥＤＴＡ无影响．
Phospholipase hydrolyzing phosphoenolpyruvate was partially purified from rice leaves with a Km (PEP) of 0.1 mmol / L and an optimum pH of 5.3. Under acidic pH conditions (PH4.0 ~ 7.2) stable, but also more stable to heat. Pi activity is strongly inhibited by Pi. It is not specific to its substrate, can hydrolyze a variety of compounds containing phosphorus ester bonds. It is a nonspecific acidic phosphatase. Metabolites of various phosphorus-containing ester bonds competitively inhibit enzyme activity and exhibit additive properties. The activities of Cu (2 +), Zn (2+) and Fe (2+) inhibitory enzymes were not affected by Mg (2 +), Mn (2+), Ca (2+), Co (2+) and EDTA.