甲基谷胱甘肽 | 34286-34-5

• 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: 甲基谷胱甘肽
• 英文名称: γ-L-glutamyl-L-cysteinyl-L-alanine
• 英文别名: γGlu-Cys-Ala；homoglutathione；methylglutathione；gamma-Glutamylcysteinylalanine；(2S)-2-amino-5-[[(2R)-1-[[(1S)-1-carboxyethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-5-oxopentanoic acid
• CAS: 34286-34-5
• 化学式: C₁₁H₁₉N₃O₆S
• 分子量: 321.354
• InChiKey: UTYLFDUOWWLTBM-ACZMJKKPSA-N

物化性质

• 沸点：
  736.1±60.0 °C(Predicted)
• 密度：
  1.396±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  21
• 可旋转键数：
  9
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.64
• 拓扑面积：
  160
• 氢给体数：
  6
• 氢受体数：
  8

反应信息

• 作为反应物：
  描述：

  甲基谷胱甘肽 在 盐酸 作用下， 反应 10.17h， 生成
  参考文献：
  名称：

  Use of L ‐[ ¹⁵ N] glutamic acid and homoglutathione to determine both glutathione synthesis and concentration by gas chromatography‐mass spectrometry (GCMS)

  摘要：

  描述了一种使用气相色谱质谱法同时测量生物样品中谷胱甘肽富集和浓度的方法。该方法基于谷胱甘肽 N,S-乙氧基羰基甲酯衍生物的制备，并使用高谷胱甘肽（谷氨酰-半胱氨酰-丙氨酸）作为内标。还报道了测定谷氨酸浓度和富集的程序。两种方法的日内和日间分析间变异系数均小于 5%，已知添加量的谷胱甘肽和谷氨酸的回收率接近 100%。总而言之，这些方法允许使用 L-[15N] 谷氨酸输注测定红细胞中的谷胱甘肽浓度和分数合成率。该方法应用于体内，以研究与对照过夜禁食相比，72 小时禁食对单只狗红细胞谷胱甘肽的影响。 72 小时禁食与红细胞谷胱甘肽水平下降 39% 相关（2.9 ± 0.4 与 4.7 ± 0.5 mmol l−1，禁食与对照），而谷胱甘肽合成分数没有变化（67.4% 与 71.3% d−1，禁食）与对照）。版权所有 © 2001 约翰威利父子有限公司

  DOI：

  10.1002/jms.185
• 作为产物：
  描述：

  L-丙氨酸 、 5-L-谷氨酰-L-半胱氨酸 在 磷烯醇丙酮酸 、 adenosine 5'-triphosphate disodium salt hydrate 、 β-nicotinamideadenine dinucleotide, reduced disodium salt hydrate 、 glutathione synthetase mutant F₁₅₂G 、 type II rabbit muscle lactate dehydrogenase 、 type II rabbit muscle pyruvate kinase 作用下， 以 aq. buffer 为溶剂， 反应 2.0h， 生成 甲基谷胱甘肽
  参考文献：
  名称：

  Metabolic Synthesis of Clickable Glutathione for Chemoselective Detection of Glutathionylation

  摘要：

  Glutathionylation involves reversible protein cysteine modification that regulates the function of numerous proteins in response to redox stimuli, thereby altering cellular processes. Herein we developed a selective and versatile approach to identifying glutathionylation by using a mutant of glutathione synthetase (GS). GS wild-type catalyzes coupling of γGlu-Cys to Gly to form glutathione. We generated a GS mutant that catalyzes azido-Ala in place of Gly with high catalytic efficiency and selectivity. Transfection of this GS mutant (F152A/S151G) and incubation of azido-Ala in cells efficiently afford the azide-containing glutathione derivative, γGlu-Cys-azido-Ala. Upon H2O2 treatment, clickable glutathione allowed for selective and sensitive detection of glutathionylated proteins by Western blotting or fluorescence after click reaction with biotin-alkyne or rhodamine-alkyne. This approach affords the efficient metabolic tagging of intracellular glutathione with small clickable functionality, providing a versatile handle for characterizing glutathionylation.

  DOI：

  10.1021/ja503946q

文献信息

• Synthesis of Hydroxymethylglutathione from Glutathione and<scp>L</scp>-Serine Catalyzed by Carboxypeptidase Y
  作者：Ryosuke OKUMURA、Yukio KOIZUMI、Jiro SEKIYA

  DOI：10.1271/bbb.67.434

  日期：2003.1

  found that carboxypeptidase Y (CPY), but not carboxypeptidase A, catalyzed hmGSH synthesis from glutathione and L-serine in vitro at acidic pH. CPY also catalyzed methylglutathione synthesis from glutathione and L-alanine. These findings suggested that a carboxypeptidase-like enzyme may be involved in hmGSH synthesis in vivo.

  羟甲基谷胱甘肽（γ-L-谷氨酰基-L-半胱氨酸-L-丝氨酸； hmGSH）存在于属于禾本科的许多物种中，但尚未发现hmGSH的生物合成途径。我们发现羧肽酶Y（CPY）而不是羧肽酶A可以在酸性pH下催化谷胱甘肽和L-丝氨酸合成hmGSH。CPY还催化由谷胱甘肽和L-丙氨酸合成甲基谷胱甘肽。这些发现表明，羧肽酶样酶可能与体内hmGSH的合成有关。
• Methods of identifying compounds that induce expression of glutathione S-transferase
  申请人：——

  公开号：US20040143869A1

  公开（公告）日：2004-07-22

  This invention relates to glutathione transferase (GST) subunits to nucleic acid sequences encoding glutathione transferase subunits, and to uses of these glutathione transferase and coding sequences, especially in the field of plant biotechnology.

  本发明涉及谷胱甘肽转移酶（GST）亚基、编码谷胱甘肽转移酶亚基的核酸序列以及这些谷胱甘肽转移酶和编码序列的用途，特别是在植物生物技术领域。
• US6730828B1
  申请人：——

  公开号：US6730828B1

  公开（公告）日：2004-05-04
• Metabolic Synthesis of Clickable Glutathione for Chemoselective Detection of Glutathionylation
  作者：Kusal T. G. Samarasinghe、Dhanushka N. P. Munkanatta Godage、Garrett C. VanHecke、Young-Hoon Ahn

  DOI：10.1021/ja503946q

  日期：2014.8.20

  Glutathionylation involves reversible protein cysteine modification that regulates the function of numerous proteins in response to redox stimuli, thereby altering cellular processes. Herein we developed a selective and versatile approach to identifying glutathionylation by using a mutant of glutathione synthetase (GS). GS wild-type catalyzes coupling of γGlu-Cys to Gly to form glutathione. We generated a GS mutant that catalyzes azido-Ala in place of Gly with high catalytic efficiency and selectivity. Transfection of this GS mutant (F152A/S151G) and incubation of azido-Ala in cells efficiently afford the azide-containing glutathione derivative, γGlu-Cys-azido-Ala. Upon H2O2 treatment, clickable glutathione allowed for selective and sensitive detection of glutathionylated proteins by Western blotting or fluorescence after click reaction with biotin-alkyne or rhodamine-alkyne. This approach affords the efficient metabolic tagging of intracellular glutathione with small clickable functionality, providing a versatile handle for characterizing glutathionylation.
• Use of <scp>L</scp> ‐[ ¹⁵ N] glutamic acid and homoglutathione to determine both glutathione synthesis and concentration by gas chromatography‐mass spectrometry (GCMS)
  作者：Bernard Humbert、Patrick Nguyen、Christiane Obled、Christine Bobin、Anne Vaslin、Shawn Sweeten、Dominique Darmaun

  DOI：10.1002/jms.185

  日期：2001.7

  A method for simultaneous measurement of both glutathione enrichment and concentration in a biological sample using gas chromatography mass spectrometry is described. The method is based on the preparation of N,S-ethoxycarbonylmethyl ester derivatives of glutathione, and the use of homoglutathione (glutamyl–cysteinyl–alanine) as an internal standard. A procedure for determination of glutamate concentration and enrichment is also reported. Both methods have within-day and day-to-day inter-assay coefficients of variation less than 5%, and recoveries of known added amounts of glutathione and glutamate are close to 100%. Taken together, these methods allowed determination of glutathione concentration and fractional synthesis rate in red blood cells using L-[15N] glutamic acid infusion. This approach was applied in vivo to investigate the effects of a 72 h fast, compared with a control overnight fast, on erythrocyte glutathione in a single dog. The 72 h fast was associated with a 39% decline in erythrocyte glutathione level, (2.9 ± 0.4 versus 4.7 ± 0.5 mmol l−1, fasting versus control) with no change in glutathione fractional synthesis (67.4 versus 71.3% d−1, fasting versus control). Copyright © 2001 John Wiley & Sons, Ltd.

  描述了一种使用气相色谱质谱法同时测量生物样品中谷胱甘肽富集和浓度的方法。该方法基于谷胱甘肽 N,S-乙氧基羰基甲酯衍生物的制备，并使用高谷胱甘肽（谷氨酰-半胱氨酰-丙氨酸）作为内标。还报道了测定谷氨酸浓度和富集的程序。两种方法的日内和日间分析间变异系数均小于 5%，已知添加量的谷胱甘肽和谷氨酸的回收率接近 100%。总而言之，这些方法允许使用 L-[15N] 谷氨酸输注测定红细胞中的谷胱甘肽浓度和分数合成率。该方法应用于体内，以研究与对照过夜禁食相比，72 小时禁食对单只狗红细胞谷胱甘肽的影响。 72 小时禁食与红细胞谷胱甘肽水平下降 39% 相关（2.9 ± 0.4 与 4.7 ± 0.5 mmol l−1，禁食与对照），而谷胱甘肽合成分数没有变化（67.4% 与 71.3% d−1，禁食）与对照）。版权所有 © 2001 约翰威利父子有限公司