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首页> 外文OA文献 >Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.) 1
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Purification and Properties of Phosphoenolpyruvate Carboxylase from Immature Pods of Chickpea (Cicer arietinum L.) 1

机译：鹰嘴豆（Cicer arietinum L.）1的未成熟荚果中磷酸烯醇丙酮酸羧化酶的纯化和性质

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摘要

Phosphoenolpyruvate carboxylase (EC 4.1.1.31) was purified to homogeneity with about 29% recovery from immature pods of chickpea using ammonium sulfate fractionation, DEAE-cellulose chromatography, and gel filtration through Sephadex G-200. The purified enzyme with molecular weight of about 200,000 daltons was a tetramer of four identical subunits and exhibited maximum activity at pH 8.1. Mg2+ ions were specifically required for the enzyme activity. The enzyme showed typical hyperbolic kinetics with phosphoenolpyruvate with a Km of 0.74 millimolar, whereas sigmoidal response was observed with increasing concentrations of HCO3− with S0.5 value as 7.6 millimolar. The enzyme was activated by inorganic phosphate and phosphate esters like glucose-6-phosphate, α-glycerophosphate, 3-phosphoglyceric acid, and fructose-1,6-bisphosphate, and inhibited by nucleotide triphosphates, organic acids, and divalent cations Ca2+ and Mn2+. Oxaloacetate and malate inhibited the enzyme noncompetitively. Glucose-6-phosphate reversed the inhibitory effects of oxaloacetate and malate.
机译：使用硫酸铵分级分离，DEAE-纤维素色谱和通过Sephadex G-200进行凝胶过滤，从未成熟的鹰嘴豆荚中回收磷酸烯醇丙酮酸羧化酶（EC 4.1.1.31）至大约29％。分子量约为200,000道尔顿的纯化酶是四个相同亚基的四聚体，在pH 8.1时表现出最大活性。 Mg2 +离子是酶活性特别需要的。该酶表现出典型的双曲动力学，磷酸烯醇丙酮酸盐的Km为0.74毫摩尔，而随着HCO3-浓度的增加，S0.5值为7.6毫摩尔，观察到了S型反应。该酶被无机磷酸酯和磷酸酯活化，如葡萄糖-6-磷酸酯，α-甘油磷酸酯，3-磷酸甘油酸和果糖-1,6-双磷酸酯，并被核苷酸三磷酸酯，有机酸和二价阳离子Ca2 +和Mn2 +抑制。 。草酰乙酸和苹果酸非竞争性抑制酶。 6-磷酸葡萄糖逆转了草酰乙酸和苹果酸的抑制作用。

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