N5-((R)-1-((2-((3-((4-aminobutyl)amino)propyl)amino)-2-oxoethyl)amino)-3-(((R)-2-hydroxypropanoyl)thio)-1-oxopropan-2-yl)-L-glutamine | 1002754-96-2

• 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: N5-((R)-1-((2-((3-((4-aminobutyl)amino)propyl)amino)-2-oxoethyl)amino)-3-(((R)-2-hydroxypropanoyl)thio)-1-oxopropan-2-yl)-L-glutamine
• CAS: 1002754-96-2
• 化学式: C₂₀H₃₈N₆O₇S
• 分子量: 506.624
• InChiKey: HFERUVOBVSGHEV-ILXRZTDVSA-N

物化性质

• 沸点：
  889.7±65.0 °C(Predicted)
• 密度：
  1.276±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -2.75
• 重原子数：
  34.0
• 可旋转键数：
  19.0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  225.97
• 氢给体数：
  8.0
• 氢受体数：
  10.0

反应信息

• 作为反应物：
  描述：

  N5-((R)-1-((2-((3-((4-aminobutyl)amino)propyl)amino)-2-oxoethyl)amino)-3-(((R)-2-hydroxypropanoyl)thio)-1-oxopropan-2-yl)-L-glutamine 在 Escherichia coli glyoxalase II 作用下， 反应 1.0h， 生成 乳酸 、 (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：

  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：

  (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