(2S)-2-氨基-5-[[2-[3-(4-氨基丁基氨基)丙基氨基]乙酰基]-[(2R)-2-氨基-3-硫基丙酰]氨基]-5-氧代戊酸 | 33932-35-3

• 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
• 中文名称: (2S)-2-氨基-5-[[2-[3-(4-氨基丁基氨基)丙基氨基]乙酰基]-[(2R)-2-氨基-3-硫基丙酰]氨基]-5-氧代戊酸
• 英文名称: N¹-Mono-glutathionylspermidine
• 英文别名: glutathionylspermidine；(2S)-2-amino-5-[[(2R)-1-[[2-[3-(4-aminobutylamino)propylamino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 33932-35-3
• 化学式: C₁₇H₃₄N₆O₅S
• 分子量: 434.56
• InChiKey: NEDQLXHBVHSKNV-STQMWFEESA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -5
• 重原子数：
  29
• 可旋转键数：
  17
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.76
• 拓扑面积：
  190
• 氢给体数：
  8
• 氢受体数：
  9

制备方法与用途

谷胱甘肽亚精胺是一种由大肠杆菌产生的肽和代谢产物。

反应信息

• 作为反应物：
  描述：

  (2S)-2-氨基-5-[[2-[3-(4-氨基丁基氨基)丙基氨基]乙酰基]-[(2R)-2-氨基-3-硫基丙酰]氨基]-5-氧代戊酸 在 Escherichia coli glyoxalase I 作用下， 生成 N5-((R)-1-((2-((3-((4-aminobutyl)amino)propyl)amino)-2-oxoethyl)amino)-3-(((R)-2-hydroxypropanoyl)thio)-1-oxopropan-2-yl)-L-glutamine
  参考文献：
  名称：

  Ni2+-activated glyoxalase I from Escherichia coli: Substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily

  摘要：

  The Escherichia coli glyoxalase system consists of the metalloenzymes glyoxalase I and glyoxalase II. Little is known regarding Ni2+-activated E. coli glyoxalase I substrate specificity, its thiol cofactor preference, the presence or absence of any substrate kinetic isotope effects on the enzyme mechanism, or whether glyoxalase I might catalyze additional reactions similar to those exhibited by related beta alpha beta beta beta structural superfamily members. The current investigation has shown that this two-enzyme system is capable of utilizing the thiol cofactors glutathionylspermidine and trypanothione, in addition to the known tripeptide glutathione, to convert substrate methylglyoxal to non-toxic D-lactate in the presence of Ni2+ ion. E. coli glyoxalase I, reconstituted with either Ni2+ or Cd2+, was observed to efficiently process deuterated and non-deuterated phenylglyoxal utilizing glutathione as cofactor. Interestingly, a substrate kinetic isotope effect for the Ni2+-substituted enzyme was not detected; however, the proton transfer step was observed to be partially rate limiting for the Cd2+-substituted enzyme. This is the first non-Zn2+-activated GlxI where a metal ion-dependent kinetic isotope effect using deuterium-labelled substrate has been observed. Attempts to detect a glutathione conjugation reaction with the antibiotic fosfomycin, similar to the reaction catalyzed by the related superfamily member FosA, were unsuccessful when utilizing the E. coli glyoxalase I E56A mutein. (c) 2011 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.jinorgbio.2011.11.008
• 作为产物：
  描述：

  5-(2,5-二氧代-1-吡咯烷基)1-(2-甲基-2-丙基)N-{[(2-甲基-2-丙基)氧基]羰基}-L-谷氨酸 在 N,N'-二环己基碳二亚胺 、 三氟乙酸 、 1,4-二巯基-2,3-丁二醇 作用下， 以 四氢呋喃 、 N,N-二甲基甲酰胺 为溶剂， 反应 26.75h， 生成 (2S)-2-氨基-5-[[2-[3-(4-氨基丁基氨基)丙基氨基]乙酰基]-[(2R)-2-氨基-3-硫基丙酰]氨基]-5-氧代戊酸
  参考文献：
  名称：

  锥虫代谢产物锥虫硫醚，N 1-单-和N 8-单-谷胱甘肽亚精胺的合成

  摘要：

  锥虫的代谢产物锥虫[ N 1，N 8-双（谷胱甘肽）亚精胺]及其生物合成代谢物，N 1-和N 8-单-谷胱甘肽亚精胺异构体是通过温和的途径合成的，该方法涉及偶联甘氨酰基-亚精胺衍生物功能保护的γ-谷氨酰半胱氨酸二肽。

  DOI：

  10.1039/c39860000593

文献信息

• Pathway Analysis of Cell Culture Phenotypes and Uses Thereof
  申请人：Melville Mark

  公开号：US20090186358A1

  公开（公告）日：2009-07-23

  The present invention provides methods for systematically identifying genes, proteins and/or related pathways that regulate or indicative of cell phenotypes. The present invention further provides methods for manipulating the identified genes, proteins and/or pathways to engineer improved cell lines and/or to evaluate or select cell lines with desirable phenotypes.
• Ni2+-activated glyoxalase I from Escherichia coli: Substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily
  作者：Kadia Y. Mullings、Nicole Sukdeo、Uthaiwan Suttisansanee、Yanhong Ran、John F. Honek

  DOI：10.1016/j.jinorgbio.2011.11.008

  日期：2012.3

  The Escherichia coli glyoxalase system consists of the metalloenzymes glyoxalase I and glyoxalase II. Little is known regarding Ni2+-activated E. coli glyoxalase I substrate specificity, its thiol cofactor preference, the presence or absence of any substrate kinetic isotope effects on the enzyme mechanism, or whether glyoxalase I might catalyze additional reactions similar to those exhibited by related beta alpha beta beta beta structural superfamily members. The current investigation has shown that this two-enzyme system is capable of utilizing the thiol cofactors glutathionylspermidine and trypanothione, in addition to the known tripeptide glutathione, to convert substrate methylglyoxal to non-toxic D-lactate in the presence of Ni2+ ion. E. coli glyoxalase I, reconstituted with either Ni2+ or Cd2+, was observed to efficiently process deuterated and non-deuterated phenylglyoxal utilizing glutathione as cofactor. Interestingly, a substrate kinetic isotope effect for the Ni2+-substituted enzyme was not detected; however, the proton transfer step was observed to be partially rate limiting for the Cd2+-substituted enzyme. This is the first non-Zn2+-activated GlxI where a metal ion-dependent kinetic isotope effect using deuterium-labelled substrate has been observed. Attempts to detect a glutathione conjugation reaction with the antibiotic fosfomycin, similar to the reaction catalyzed by the related superfamily member FosA, were unsuccessful when utilizing the E. coli glyoxalase I E56A mutein. (c) 2011 Elsevier Inc. All rights reserved.
• Synthesis of the trypanosomatid metabolites trypanothione, and N 1-mono- and N 8-mono-glutathionylspermidine
  作者：Graeme B. Henderson、Peter Ulrich、Alan H. Fairlamb、Anthony Cerami

  DOI：10.1039/c39860000593

  日期：——

  The trypanosomatid metabolite trypanothione [N1,N8-bis(glutathionyl)spermidine] and its biosynthetic co-metabolites the isomeric N1- and N8-mono-glutathionylspermidines have been synthesised by a mild route which involves coupling of glycinyl-spermidine derivatives to a functionally protected γ-glutamylcysteine dipeptide.

  锥虫的代谢产物锥虫[ N 1，N 8-双（谷胱甘肽）亚精胺]及其生物合成代谢物，N 1-和N 8-单-谷胱甘肽亚精胺异构体是通过温和的途径合成的，该方法涉及偶联甘氨酰基-亚精胺衍生物功能保护的γ-谷氨酰半胱氨酸二肽。