Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata)
Kinetic mechanism and order of substrate binding for sn-glycerol-3-phosphate acyltransferase from squash (Cucurbita moschata)
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DOI：
10.1016/s0014-5793(02)02381-5
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发表时间：
2002-03-13
期刊：
影响因子：
3.5
通讯作者：
Slabas, AR
中科院分区：
文献类型：
--
作者：
Hayman, MW;Fawcett, T;Slabas, AR
sn-甘油-3-磷酸酰基转移酶（glycerol-3-phosphate acyltransferase，G3 PAT，EC 2.3.1.15）是植物体内甘油脂合成的一个组分，是植物对低温敏感性的一个重要酶。已经确定了来自南瓜（南瓜（Cucurbita moschata））的酶的三维结构，没有结合的底物[Turnbull等人（2001）Acta Crystallogr. D 57，451-453; Turnbull等人（2001）Structure 9，347-353]。在这里，我们报告的动力学机制的质体G3 PAT从南瓜和基板结合使用酰基-酰基载体蛋白（酰基-ACP）基板的顺序。该反应通过在甘油-3-磷酸之前与酰基-ACP结合的强制有序三元复合物进行。我们还确定了反应将使用C-4：0-CoA、C-6：0-CoA和C-12：0-ACP底物进行，从而为未来的共结晶研究提供了更广泛的酰基选择。(C)2002年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
sn-Glycerol-3-phosphate acyltransferase (G3PAT, EC 2.3.1.15), a component of glycerolipid biosynthesis, is an important enzyme in chilling sensitivity in plants. The three-dimensional structure of the enzyme from squash (Cucurbita moschata), without bound substrate, has been determined [Turnbull et al. (2001) Acta Crystallogr. D 57, 451-453; Turnbull et al. (2001) Structure 9, 347-353]. Here we report the kinetic mechanism of plastidial G3PAT from squash and the order of substrate binding using acyl-acyl carrier protein (acyl-ACP) substrates. The reaction proceeds via a compulsory-ordered ternary complex with acyl-ACP binding before glycerol-3-phosphate. We have also determined that the reaction will proceed with C-4:0-CoA, C-6:0-CoA and C-12:0-ACP substrates, allowing a wider choice of acyl groups for future co-crystallisation studies. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.