A single amino acid determines position specificity of an Arabidopsis thaliana CCoAOMT-like O-methyltransferase
A single amino acid determines position specificity of an Arabidopsis thaliana CCoAOMT-like O-methyltransferase
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DOI：
10.1016/j.febslet.2013.01.040
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发表时间：
2013-03-18
期刊：
影响因子：
3.5
通讯作者：
Vogt, Thomas
中科院分区：
文献类型：
--
作者：
Wils, Christopher Ralf;Brandt, Wolfgang;Vogt, Thomas
来自植物的咖啡酰辅酶AO-甲基转移酶（CCoAOMT）样蛋白对芳香邻二羟基的间位表现出保守的位置特异性，与体内观察到的甲基化模式一致。从拟南芥中鉴定出的由 At4g26220 基因编码的 CCoAOMT 样酶显示出对黄烷酮和二氢黄酮醇对位甲基化的强烈偏好，而黄酮和黄酮醇在间位甲基化。与其他 CCoAOMT 样酶的基序相比，序列比对和同源性建模确定了几个独特的氨基酸。单个甘氨酸 G46 向酪氨酸的突变足以逆转黄烷酮和二氢黄酮醇的异常对位甲基化。 (C) 2013 年欧洲生化学会联合会。由 Elsevier B.V. 出版。保留所有权利。
Caffeoyl-coenzymeAO-methyltransferase (CCoAOMT)-like proteins from plants display a conserved position specificity towards the meta-position of aromatic vicinal dihydroxy groups, consistent with the methylation pattern observed in vivo. A CCoAOMT-like enzyme identified from Arabidopsis thaliana encoded by the gene At4g26220 shows a strong preference for methylating the para position of flavanones and dihydroflavonols, whereas flavones and flavonols are methylated in the meta-position. Sequence alignments and homology modelling identified several unique amino acids compared to motifs of other CCoAOMT-like enzymes. Mutation of a single glycine, G46 towards a tyrosine was sufficient for a reversal of the unusual para-back to meta-O-methylation of flavanones and dihydroflavonols. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.