Induction of hydroxyanthranilate hydroxycinnamoyl transferase activity by oligo-N-acetylchitooligosaccharides in oats
Induction of hydroxyanthranilate hydroxycinnamoyl transferase activity by oligo-N-acetylchitooligosaccharides in oats
复制标题
DOI：
10.1016/s0031-9422(97)00603-1
复制
发表时间：
1998-03-01
期刊：
影响因子：
3.8
通讯作者：
Iwamura, H
中科院分区：
文献类型：
--
作者：
Ishihara, A;Miyagawa, H;Iwamura, H
一种燕麦叶（Avena sativa L.）中羟基肉桂酰辅酶A：羟基邻氨基苯甲酸N-羟基肉桂酰转移酶（HHT）的测定方法，该酶被认为是该植物中植物抗毒素燕麦生物碱生物合成的关键酶之一。用低聚N-乙酰壳寡糖处理叶片诱导HHT活性。在所测试的壳寡糖中，五-N-乙酰基壳五糖（（GlcNAc）（5））在诱导活性方面是最有效的。（GlcNAc）（5）的诱导具有剂量依赖性，在这种情况下，HHT活性最初在6小时后检测到，并在12小时时达到最大值。燕麦蒽醌的所有推定前体均作为HHT的底物，5-羟基邻氨基苯甲酸和阿魏酰辅酶A分别是燕麦蒽醌的邻氨基苯甲酸部分和肉桂酰部分的最佳底物。(C)1998爱思唯尔科技有限公司版权所有。
An assay method for hydroxycinnamoyl-CoA: hydroxyanthranilate N-hydroxycinnamoyl transferase (HHT) in oat leaves (Avena sativa L.), which is thought to be one of the key enzymes for the biosynthesis of avenanthramides, phytoalexins in this plant, was established. HHT activity was induced by treating the leaves with oligo-N-acetylchitooligosaccharides. Among the chitooligosaccharides tested, penta-N-acetylchitopentaose ((GlcNAc)(5)) was the most effective in inducing activity. The induction by (GlcNAc)(5) was dose-dependent, in which case HHT activity was initially detected after 6 hr and reached a maximum by 12 hr. All of the putative precursors of avenanthramides acted as substrates for HHT, with 5-hydroxyanthranilic acid and feruloyl-CoA being the best substrates for the anthranilic moiety and the cinnamoyl moiety of avenanthramides, respectively. (C) 1998 Elsevier Science Ltd. All rights reserved.