N,N-dihydroxy-L-trihomomethionine

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: N,N-dihydroxy-L-trihomomethionine
• 英文别名: (2S)-2-(dihydroxyamino)-7-methylsulfanylheptanoate
• 化学式: C8H16NO4S-
• 分子量: 222.28
• InChiKey: PBLLFERESQOVTJ-ZETCQYMHSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -0.6
• 重原子数：
  14
• 可旋转键数：
  7
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.88
• 拓扑面积：
  109
• 氢给体数：
  2
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  氢(+1)阳离子 、 N,N-dihydroxy-L-trihomomethionine 生成 6-Methylthiohexanaldoxime 、 二氧化碳 、 水
  参考文献：
  名称：

  Cytochrome P450 CYP79F1 from Arabidopsis Catalyzes the Conversion of Dihomomethionine and Trihomomethionine to the Corresponding Aldoximes in the Biosynthesis of Aliphatic Glucosinolates

  摘要：

  Glucosinolates are natural plant products that have received rising attention due to their role in interactions between pests and crop plants and as chemical protectors against cancer. Glucosinolates are derived from amino acids and have aldoximes as intermediates. We report that cytochrome P450 CYP79F1 catalyzes aldoxime:formation in the biosynthesis of aliphatic glucosinolates in Arabidopsis thaliana. Using recombinant CYP79F1 functionally expressed in Escherichia coli, we show that both dihomomethionine and trihomomethionine are metabolized by CYP79F1 resulting in the formation of 5-methylthiopentanaldoxime and 6-methylthiohexanaldoxime, respectively. 5-methylthiopentanaldoxime is the precursor of the major glucosinolates in leaves of A. thaliana, i.e. 4-methylthiobutylglucosinolate and 4-methylsulfinylbutylglucosinolate, and a variety of other glucosinolates in Brassica sp, Transgenic A. thaliana with cosuppression of CYP79F1 have a reduced content of aliphatic glucosinolates and a highly increased level of dihomomethionine and trihomomethionine. The transgenic plants have a morphological phenotype showing loss of apical dominance and formation of multiple axillary shoots. Our data provide the first evidence that a cytochrome P450 catalyzes the N-hydroxylation of chain-elongated methionine homologues to the corresponding aldoximes in the biosynthesis of aliphatic glucosinolates.

  DOI：

  10.1074/jbc.m010123200
• 作为产物：
  描述：

  N-hydroxy-L-trihomomethionine 、 氧气 、 1-Deoxy-1-(7,8-dimethyl-2,4-dioxidobenzo[g]pteridin-10(5H)-yl)-5-O-phosphonopentitol 生成 氢(+1)阳离子 、 水 、 N,N-dihydroxy-L-trihomomethionine 、 FMN
  参考文献：
  名称：

  Cytochrome P450 CYP79F1 from Arabidopsis Catalyzes the Conversion of Dihomomethionine and Trihomomethionine to the Corresponding Aldoximes in the Biosynthesis of Aliphatic Glucosinolates

  摘要：

  Glucosinolates are natural plant products that have received rising attention due to their role in interactions between pests and crop plants and as chemical protectors against cancer. Glucosinolates are derived from amino acids and have aldoximes as intermediates. We report that cytochrome P450 CYP79F1 catalyzes aldoxime:formation in the biosynthesis of aliphatic glucosinolates in Arabidopsis thaliana. Using recombinant CYP79F1 functionally expressed in Escherichia coli, we show that both dihomomethionine and trihomomethionine are metabolized by CYP79F1 resulting in the formation of 5-methylthiopentanaldoxime and 6-methylthiohexanaldoxime, respectively. 5-methylthiopentanaldoxime is the precursor of the major glucosinolates in leaves of A. thaliana, i.e. 4-methylthiobutylglucosinolate and 4-methylsulfinylbutylglucosinolate, and a variety of other glucosinolates in Brassica sp, Transgenic A. thaliana with cosuppression of CYP79F1 have a reduced content of aliphatic glucosinolates and a highly increased level of dihomomethionine and trihomomethionine. The transgenic plants have a morphological phenotype showing loss of apical dominance and formation of multiple axillary shoots. Our data provide the first evidence that a cytochrome P450 catalyzes the N-hydroxylation of chain-elongated methionine homologues to the corresponding aldoximes in the biosynthesis of aliphatic glucosinolates.

  DOI：

  10.1074/jbc.m010123200

文献信息

• CYP79F1 and CYP79F2 have distinct functions in the biosynthesis of aliphatic glucosinolates in Arabidopsis
  作者：Sixue Chen、Erich Glawischnig、Kirsten Jørgensen、Peter Naur、Bodil Jørgensen、Carl-Erik Olsen、Carsten H. Hansen、Hasse Rasmussen、John A. Pickett、Barbara A. Halkier

  DOI：10.1046/j.1365-313x.2003.01679.x

  日期：2003.3

  SummaryCytochromes P450 of the CYP79 family catalyze the conversion of amino acids to oximes in the biosynthesis of glucosinolates, a group of natural plant products known to be involved in plant defense and as a source of flavor compounds, cancer‐preventing agents and bioherbicides. We report a detailed biochemical analysis of the substrate specificity and kinetics of CYP79F1 and CYP79F2, two cytochromes P450 involved in the biosynthesis of aliphatic glucosinolates in Arabidopsis thaliana. Using recombinant CYP79F1 and CYP79F2 expressed in Escherichia coli and Saccharomyces cerevisiae, respectively, we show that CYP79F1 metabolizes mono‐ to hexahomomethionine, resulting in both short‐ and long‐chain aliphatic glucosinolates. In contrast, CYP79F2 exclusively metabolizes long‐chain elongated penta‐ and hexahomomethionines. CYP79F1 and CYP79F2 are spatially and developmentally regulated, with different gene expression patterns. CYP79F2 is highly expressed in hypocotyl and roots, whereas CYP79F1 is strongly expressed in cotyledons, rosette leaves, stems, and siliques. A transposon‐tagged CYP79F1 knockout mutant completely lacks short‐chain aliphatic glucosinolates, but has an increased level of long‐chain aliphatic glucosinolates, especially in leaves and seeds. The level of long‐chain aliphatic glucosinolates in a transposon‐tagged CYP79F2 knockout mutant is substantially reduced, whereas the level of short‐chain aliphatic glucosinolates is not affected. Biochemical characterization of CYP79F1 and CYP79F2, and gene expression analysis, combined with glucosinolate profiling of knockout mutants demonstrate the functional role of these enzymes. This provides valuable insights into the metabolic network leading to the biosynthesis of aliphatic glucosinolates, and into metabolic engineering of altered aliphatic glucosinolate profiles to improve nutritional value and pest resistance.
• Cytochrome P450 CYP79F1 from Arabidopsis Catalyzes the Conversion of Dihomomethionine and Trihomomethionine to the Corresponding Aldoximes in the Biosynthesis of Aliphatic Glucosinolates
  作者：Carsten Hørslev Hansen、Ute Wittstock、Carl Erik Olsen、Alastair J. Hick、John A. Pickett、Barbara Ann Halkier

  DOI：10.1074/jbc.m010123200

  日期：2001.4

  Glucosinolates are natural plant products that have received rising attention due to their role in interactions between pests and crop plants and as chemical protectors against cancer. Glucosinolates are derived from amino acids and have aldoximes as intermediates. We report that cytochrome P450 CYP79F1 catalyzes aldoxime:formation in the biosynthesis of aliphatic glucosinolates in Arabidopsis thaliana. Using recombinant CYP79F1 functionally expressed in Escherichia coli, we show that both dihomomethionine and trihomomethionine are metabolized by CYP79F1 resulting in the formation of 5-methylthiopentanaldoxime and 6-methylthiohexanaldoxime, respectively. 5-methylthiopentanaldoxime is the precursor of the major glucosinolates in leaves of A. thaliana, i.e. 4-methylthiobutylglucosinolate and 4-methylsulfinylbutylglucosinolate, and a variety of other glucosinolates in Brassica sp, Transgenic A. thaliana with cosuppression of CYP79F1 have a reduced content of aliphatic glucosinolates and a highly increased level of dihomomethionine and trihomomethionine. The transgenic plants have a morphological phenotype showing loss of apical dominance and formation of multiple axillary shoots. Our data provide the first evidence that a cytochrome P450 catalyzes the N-hydroxylation of chain-elongated methionine homologues to the corresponding aldoximes in the biosynthesis of aliphatic glucosinolates.