Activities of acyl-CoA:diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT) in microsomal preparations of developing sunflower and safflower seeds.

Activities of acyl-CoA:diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT) in microsomal preparations of developing sunflower and safflower seeds.
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DOI:
10.1007/s00425-013-1870-8
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发表时间:
2013-06
期刊:
影响因子:
4.3
通讯作者:
Stymne S
Stymne S
中科院分区:
生物学2区
文献类型:
--
作者:
Banaś W;Sanchez Garcia A;Banaś A;Stymne S

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油料种子中三酰基甘油(TAG)生物合成的最后一步,二酰基甘油(DAG)的酰化,由两种类型的酶催化:酰基辅酶A:二酰基甘油酰基转移酶(DGAT)和磷脂:二酰基甘油酰基转移酶(PDAT)。这些酶在TAG合成中的相对贡献尚未在任何植物组织中确定。在目前的工作中,微粒体制剂获得向日葵和红花种子在不同的发展阶段,并用于DGAT和PDAT酶测定。PDAT和DGAT活性之间的比率在两个不同物种之间差异显著。DGAT活性用两种不同的酰基受体和使用两种不同的酰基辅酶A的测定方法测量,并且在所有情况下,红花中PDAT与DGAT活性的比率显著高于向日葵。通过两种方法测量的向日葵DGAT显示出与18:1-CoA相比与18:2-CoA显著更高的活性,而与红花酶观察到相反的特异性。另一方面,PDAT的特异性在两个物种中相似,18:2-磷脂酰胆碱是比18:1-PC更好的酰基供体,并且在sn-2位置的酰基的利用率约为sn-1位置的四倍。未在微粒体制备物中检测到DAG:DAG转酰酶活性。本文的在线版本(doi:10.1007/s 00425 -013-1870-8)包含补充材料,可供授权用户使用。
The last step in triacylglycerols (TAG) biosynthesis in oil seeds, the acylation of diacylglycerols (DAG), is catalysed by two types of enzymes: the acyl-CoA:diacylglycerol acyltransferase (DGAT) and phospholipid:diacylglycerol acyltransferase (PDAT). The relative contribution of these enzymes in the synthesis of TAG has not yet been defined in any plant tissue. In the presented work, microsomal preparations were obtained from sunflower and safflower seeds at different stages of development and used in DGAT and PDAT enzyme assays. The ratio between PDAT and DGAT activity differed dramatically between the two different species. DGAT activities were measured with two different acyl acceptors and assay methods using two different acyl-CoAs, and in all cases the ratio of PDAT to DGAT activity was significantly higher in safflower than sunflower. The sunflower DGAT, measured by both methods, showed significant higher activity with 18:2-CoA than with 18:1-CoA, whereas the opposite specificity was seen with the safflower enzyme. The specificities of PDAT on the other hand, were similar in both species with 18:2-phosphatidylcholine being a better acyl donor than 18:1-PC and with acyl groups at the sn-2 position utilised about fourfold the rate of the sn-1 position. No DAG:DAG transacylase activity could be detected in the microsomal preparations. The online version of this article (doi:10.1007/s00425-013-1870-8) contains supplementary material, which is available to authorized users.
DOI: 10.1046/j.1432-1327.2000.00961.x
发表时间: 2000-01-01
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