gamma-Glutamyl-glycyl-glycine | 13640-39-6

• 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: gamma-Glutamyl-glycyl-glycine
• 英文别名: γ-glutamyl-glycyl-glycine；γ-glutamylglycylglycine；H-Glu(Gly-Gly-OH)-OH；L-γ-GluGlyGly；γ-Glu-Ala-Gly；γ-Glu-Gly-Gly；H-gamma-Glu-Gly-Gly-OH；(2S)-2-amino-5-[[2-(carboxymethylamino)-2-oxoethyl]amino]-5-oxopentanoic acid
• CAS: 13640-39-6
• 化学式: C₉H₁₅N₃O₆
• 分子量: 261.235
• InChiKey: RWAZIEYJAWTKLB-YFKPBYRVSA-N

物化性质

• 熔点：
  176-178 °C
• 沸点：
  749.0±60.0 °C(Predicted)
• 密度：
  1.433±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.8
• 重原子数：
  18
• 可旋转键数：
  8
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.56
• 拓扑面积：
  159
• 氢给体数：
  5
• 氢受体数：
  7

安全信息

• 海关编码：
  2924199090

制备方法与用途

γ-Glu-Gly-Gly 是一种三肽，可以作为肽底物生成 Glu[1]。

反应信息

• 作为反应物：
  描述：

  gamma-Glutamyl-glycyl-glycine 在 recombinant Pseudomonas nitroreducens IFO12694 γ-glutamyltranspeptidase 作用下， 反应 0.03h， 生成 L-谷氨酸 、 双甘肽
  参考文献：
  名称：

  Molecular Cloning and Characterization of γ-Glutamyltranspeptidase fromPseudomonas nitroreducensIFO12694

  摘要：

  与其它γ-谷氨酰转肽酶（GGT）相比，来自IFO12694的铜绿假单胞菌（PnGGT）展现出更高的水解活性而非转移活性。PnGGT对大多数L-氨基酸和常在GGT转移反应中用作标准γ-谷氨酰受体的甘氨酰甘氨酸表现出极低活性。作为γ-谷氨酰受体，PnGGT的优先底物为甲胺、乙胺和异丙胺等胺类。

  DOI：

  10.1271/bbb.100199
• 作为产物：
  描述：

  Γ-谷氨酰-谷氨酰胺 在 recombinant Pseudomonas nitroreducens IFO12694 γ-glutamyltranspeptidase 作用下， 反应 0.36h， 生成 gamma-Glutamyl-glycyl-glycine
  参考文献：
  名称：

  Molecular Cloning and Characterization of γ-Glutamyltranspeptidase fromPseudomonas nitroreducensIFO12694

  摘要：

  与其它γ-谷氨酰转肽酶（GGT）相比，来自IFO12694的铜绿假单胞菌（PnGGT）展现出更高的水解活性而非转移活性。PnGGT对大多数L-氨基酸和常在GGT转移反应中用作标准γ-谷氨酰受体的甘氨酰甘氨酸表现出极低活性。作为γ-谷氨酰受体，PnGGT的优先底物为甲胺、乙胺和异丙胺等胺类。

  DOI：

  10.1271/bbb.100199

文献信息

• γ-Glutamyl transpeptidase acylation with peptidic substrates: free energy relationships measured by an HPLC kinetic assay
  作者：Mylène Morin、Caroline Rivard、Jeffrey W. Keillor

  DOI：10.1039/b606914b

  日期：——

  γ-Glutamyl transpeptidase (GGT, EC 2.3.2.2) is a highly glycosylated heterodimeric enzyme linked to the external cellular membrane that catalyzes the hydrolysis of glutathione as well as the transfer of its γ-glutamyl group to amino acids and dipeptides in a transpeptidation reaction. The measurement of both the hydrolytic and transpeptidation activity of this important enzyme is a challenge, since its native substrates are not highly chromogenic. We have developed an HPLC-based method for the quantitative photometric detection of numerous enzyme substrates and products, after their pre-column derivation with dabsyl chloride. The broad applicability of this method was demonstrated in the kinetic investigation of transpeptidation reactions of rat kidney GGT with glutathione, its native substrate, as well as a series of pertinent glutathione analogues. The pH-rate profile constructed for glutathione confirmed the dependence on the ionisation state of at least two residues. Analysis of the free-energy relationships in the series of synthetic peptidic substrate analogues revealed the importance of enzyme–substrate interactions unrelated to amine leaving group basicity during the acylation step. These results are further interpreted in the context of the recently published structure for a similar GGT.

  γ-谷氨酰转肽酶（GGT，EC 2.3.2.2）是一种高度糖基化的异二聚体酶，与细胞外膜相连，能够催化谷胱甘肽的水解以及在转肽反应中将其γ-谷氨酰基团转移到氨基酸和二肽上。由于其天然底物不具备高色性，因此测定这种重要酶的水解和转肽活性是一项挑战。我们开发了一种基于HPLC的方法，通过与丹磺酰氯的柱前衍生化，对多种酶底物和产物进行定量光度检测。该方法的广泛适用性在以谷胱甘肽及其一系列相关类似物为底物的鼠肾GGT转肽反应动力学研究中得到了证明。为谷胱甘肽构建的pH-速率曲线证实了其依赖于至少两种残基的离子化状态。对一系列合成肽底物类似物中的自由能关系的分析揭示了在酰化步骤中与胺离去基团碱性无关的酶-底物相互作用的重要性。这些结果进一步在最近发表的类似GGT结构的背景下进行了解释。
• Distinguishable Action between Acid-stable and Neutral α-Amylases from<i>Shochu Koji</i>(<i>Aspergillus kawachii</i>)
  作者：Toshihiko Suganuma、Naoyuki Noda、Hiroyuki Honbo、Kanefumi Kitahara

  DOI：10.1271/bbb.61.1617

  日期：1997.1

  Acid-stable (KAA) and neutral (KNA) α-amylases from shochu koji (A. kawachii) were purified and their actions towards maltooligosaccharides were studied. KAA could be distinguished from KNA by the following actions: with KAA, maltopentaose (G5) was preferentially hydrolyzed at the third glycoside bond, and the addition of potassium thiocyanate (KSCN) decreased the rate of CNP-release from 2-chloro-4-nitrophenyl-α-maltotrioside (CNP-G3).

  来自烧酒曲（A. kawachii）的酸稳定（KAA）和中性（KNA）α-淀粉酶经过纯化，并研究了它们对麦芽寡糖的作用。KAA与KNA的区别在于以下作用：对于KAA，麦芽戊糖（G5）在第三个糖苷键处优先水解，并且添加硫氰酸钾（KSCN）降低了2-氯-4-硝基苯基-α-麦芽三糖苷（CNP-G3）中CNP释放的速率。
• γ-Glutamyl Transfer Reactions by Glutaminase from<i>Pseudomonas nitroreducens</i>IFO 12694 and Their Application for the Syntheses of Theanine and γ-Glutamylmethylamide
  作者：Takashi TACHIKI、Takeshi YAMADA、Katsushige MIZUNO、Masashi UEDA、Ju-ichi SHIODE、Hiroshi FUKAMI

  DOI：10.1271/bbb.62.1279

  日期：1998.1

  In a mixture containing γ-glutamyl donor (donor) and γ-glutamyl acceptor (acceptor), the glutaminase of Pseudomonas nitroreducens IFO 12694 simultaneously catalyzed a γ-glutamyl transfer reaction and hydrolysis of the donor. The variation of the activities responding to the concentration of glutathione and glycylglycine indicated that the enzyme might be classified in a group of glutaminases that shows hydrolysis prior to transfer reaction. On the other hand, the results with glutamine and ethylamine or methylamine indicated that the enzyme was active in the transfer reaction with suppressed hydrolysis of glutamine, and suggested the possibility of using the reaction for producing γ-glutamylethylamide (theanine) or γ-glutamylmethylamide (γ-GMA). In fact, in a mixture containing high concentrations of substrates (0.7 M glutamine, 1.5 M ethylamine or methylamine) and 0.5 unit/ml glutaminase (borate buffer pH 11), 270 mM (47 g/L) theanine or 250 mM (38 g/L) γ-GMA was formed in 7 h of incubation at 30°C.

  在一混合物中，含有γ-谷氨酰供体（供体）和γ-谷氨酰受体（受体），Pseudomonas nitroreducens IFO 12694的谷氨酰胺酶同时催化γ-谷氨酰转移反应和供体的裂解。谷胱甘肽和甘氨酰甘氨酸浓度对活性的变化表明，该酶可能属于一类谷氨酰胺酶，表现出裂解优先于转移反应。另一方面，谷氨酰胺和乙胺或甲胺的结果表明，该酶在转移反应中活跃，而谷氨酰胺的裂解被抑制，这提示了利用该反应生产γ-谷氨酰乙胺（茶氨酸）或γ-谷氨酰甲胺（γ-GMA）的可能性。实际上，在高浓度底物（0.7 M谷氨酰胺，1.5 M乙胺或甲胺）和0.5单位/毫升谷氨酰胺酶（硼酸盐缓冲液pH 11）的混合物中，在30°C下孵育7小时，形成了270 mM（47 g/L）的茶氨酸或250 mM（38 g/L）的γ-GMA。
• Depth-sensing indentation at macroscopic dimensions
  作者：Jeremy Thurn、Dylan J. Morris、Robert F. Cook

  DOI：10.1557/jmr.2002.0388

  日期：2002.10

  A macroscopic-scale depth-sensing indentation apparatus with the ability to be mounted on an inverted microscope for in situ observation of contact events was calibrated using the Oliver and Pharr [J. Mater. Res. 7, 1564 (1992)] procedure with a two-parameter area function. The calibrated Vickers tip was used to determine the projected contact area at peak load and the modulus and hardness of a variety of non-metallic materials through deconvolution of the measured load-displacement traces. The predicted contact area was found to be identical to the measured area of residual contact impressions. Furthermore, for transparent ceramic materials the projected contact area during loading was found to be the same as the area measured from the diagonal of post-indentation residual contact impressions. The modulus and hardness values deconvoluted from the load–displacement traces were compared with independent measurements. The effects of sample clamping, column compliance, and tip radius on the load–displacement data and inferred materials properties were also examined. It is suggested that the simplicity of instrumentation and operation, combined with the ability to observe indentations optically, even in situ, makes macroscopic-scale depth-sensing indentation ideal for fundamental studies of contact mechanics.

  使用 Oliver 和 Pharr [J. Mater. Res. 7, 1564 (1992)]的双参数面积函数程序校准了可安装在倒置显微镜上现场观察接触事件的宏观尺度深度感应压痕仪。校准后的维氏针尖用于确定峰值载荷时的预计接触面积，以及通过对测量的载荷-位移轨迹进行解卷积来确定各种非金属材料的模量和硬度。结果发现，预测的接触面积与测量的残留接触印痕面积相同。此外，对于透明陶瓷材料，加载期间的预测接触面积与压痕后残留接触印痕对角线上测量的面积相同。从加载-位移轨迹中分解出的模量和硬度值与独立测量值进行了比较。此外，还研究了样品夹持、柱顺应性和顶端半径对载荷-位移数据和推断材料属性的影响。研究表明，仪器和操作的简易性，加上光学观测压痕的能力，甚至是原位观测的能力，使宏观尺度的深度感应压痕成为接触力学基础研究的理想选择。
• Enzymatic Synthesis of γ‐Glutamyl Dipeptides Catalysed by Mutant <i>E. coli</i> γ‐Glutamyltransferases
  作者：Marco Rabuffetti、Giovanna Speranza、Cinzia Calvio、Carlo F. Morelli

  DOI：10.1002/ejoc.202200907

  日期：2022.11.18

  identified inside the active site of E. coli γ-glutamyltransferase, putatively involved in acceptor substrate binding. Point-mutation of these residues afforded two mutant enzymes with altered catalytic properties. Mutant T413L showed a very promising transpeptidation-to-hydrolysis ratio up to 20 : 1. The two mutants were tested as biocatalysts for the enzymatic synthesis of γ-glutamyl dipeptides with flavor-enhancer

  在大肠杆菌γ-谷氨酰转移酶的活性位点内鉴定出两个残基，推测与受体底物结合有关。这些残基的点突变提供了两种催化特性改变的突变酶。突变体 T413L 显示出非常有希望的高达 20:1 的转肽水解比。这两个突变体被测试为用于酶促合成具有增味特性的 γ-谷氨酰二肽的生物催化剂。