植物全（酰基载体蛋白）合酶。
Plant holo-(acyl carrier protein) synthase.
作者信息
Elhussein S A, Miernyk J A, Ohlrogge J B
机构信息
Seed Biosynthesis Research Unit, United States Department of Agriculture, Peoria, IL 61604.
出版信息
Biochem J. 1988 May 15;252(1):39-45. doi: 10.1042/bj2520039.
Abstract
- An improved method was developed for the assay of plant holo-(acyl carrier protein) synthase activity, using Escherichia coli acyl-(acyl carrier protein) synthetase as a coupling enzyme. 2. Holo-(acyl carrier protein) synthase was partially purified from spinach (Spinacia oleracea) leaves by a combination of (NH4)2SO4 fractionation and anion-exchange and gel-permeation chromatography. 3. The partially purified enzyme had a pH optimum of 8.2 and Km values of 2 microM, 72 microM and 3 mM for apo-(acyl carrier protein), CoA and Mg2+ respectively. Synthase activity was inhibited in vitro by the reaction product 3',5'-ADP. 4. Results from the fractionation of spinach leaf and developing castor-oil-seed (Ricinus communis) endosperm cells were consistent with a cytosolic localization of holo-(acyl carrier protein) synthase activity in plant cells.
摘要
- 开发了一种改进方法，以大肠杆菌酰基-（酰基载体蛋白）合成酶作为偶联酶来测定植物全（酰基载体蛋白）合成酶活性。2. 通过硫酸铵分级分离、阴离子交换和凝胶渗透色谱相结合的方法，从菠菜（Spinacia oleracea）叶片中部分纯化了全（酰基载体蛋白）合成酶。3. 部分纯化的酶的最适pH为8.2，对脱辅基（酰基载体蛋白）、辅酶A和Mg2+的Km值分别为2微摩尔、72微摩尔和3毫摩尔。合成酶活性在体外被反应产物3'，5'-ADP抑制。4. 菠菜叶和发育中的蓖麻（Ricinus communis）胚乳细胞分级分离的结果与植物细胞中全（酰基载体蛋白）合成酶活性定位于细胞质一致。
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本文引用的文献
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A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein].一种在全[酰基载体蛋白]合成中存在条件性缺陷的大肠杆菌突变体。
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Acylation of plant acyl carrier proteins by acyl-acyl carrier protein synthetase from Escherichia coli.大肠杆菌酰基-酰基载体蛋白合成酶对植物酰基载体蛋白的酰化作用。
Arch Biochem Biophys. 1984 Apr;230(1):110-6. doi: 10.1016/0003-9861(84)90091-2.
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Turnover of the 4'-phosphopantetheine prosthetic group of acyl carrier protein.酰基载体蛋白4'-磷酸泛酰巯基乙胺辅基的周转
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