重组表硫醚特异蛋白的特性及其在拟南芥中的过量表达
Characterisation of recombinant epithiospecifier protein and its over-expression in Arabidopsis thaliana.
作者信息
Zabala Marta de Torres, Grant Murray, Bones Atle M, Bennett Richard, Lim Yin Sze, Kissen Ralph, Rossiter John T
机构信息
Department of Agricultural Sciences, Imperial College, University of London, Wye, Ashford, Kent TN25 5AH, UK.
出版信息
Phytochemistry. 2005 Apr;66(8):859-67. doi: 10.1016/j.phytochem.2005.02.026.
Epithiospecifier protein (ESP) is a protein that catalyses formation of epithionitriles during glucosinolate hydrolysis. In vitro assays with a recombinant ESP showed that the formation of epithionitriles from alkenylglucosinolates is ESP and ferrous ion dependent. Nitrile formation in vitro however does not require ESP but only the presence of Fe(II) and myrosinase. Ectopic expression of ESP in Arabidopsis thaliana Col-5 under control of the strong viral CaMV 35S promoter altered the glucosinolate product profile from isothiocyanates towards the corresponding nitriles.
表硫醚特异蛋白（ESP）是一种在硫代葡萄糖苷水解过程中催化环硫腈形成的蛋白质。对重组ESP进行的体外试验表明，由链烯基硫代葡萄糖苷形成环硫腈依赖于ESP和亚铁离子。然而，体外腈的形成并不需要ESP，仅需要Fe(II)和黑芥子酶的存在。在强病毒CaMV 35S启动子的控制下，ESP在拟南芥Col-5中的异位表达改变了硫代葡萄糖苷产物谱，从异硫氰酸酯转向相应的腈。
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