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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.