dansyl-Gly-Cys-Val-Ile-Ala

• 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: dansyl-Gly-Cys-Val-Ile-Ala
• 英文别名: N-dansyl-GCVIA；N-dansyl-Gly-Cys-Val-Ile-Ala-OH；(2S)-2-[[(2S,3S)-2-[[(2S)-2-[[(2R)-2-[[2-[[5-(dimethylamino)naphthalen-1-yl]sulfonylamino]acetyl]amino]-3-sulfanylpropanoyl]amino]-3-methylbutanoyl]amino]-3-methylpentanoyl]amino]propanoic acid
• 化学式: C₃₁H₄₆N₆O₈S₂
• 分子量: 694.874
• InChiKey: OBTFHAKXWNWAMP-PRRSXLDJSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  3
• 重原子数：
  47
• 可旋转键数：
  17
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.52
• 拓扑面积：
  213
• 氢给体数：
  7
• 氢受体数：
  11

反应信息

• 作为反应物：
  描述：

  dansyl-Gly-Cys-Val-Ile-Ala 在 carboxypeptidase Y 、 PFTase 作用下， 反应 4.0h， 生成
  参考文献：
  名称：

  Stereochemical Analysis of the Reaction Catalyzed by Yeast Protein Farnesyltransferase

  摘要：

  DOI：

  10.1021/jo980304s

文献信息

• Selective labeling of polypeptides using protein farnesyltransferase via rapid oxime ligation
  作者：Mohammad Rashidian、Jonathan K. Dozier、Stepan Lenevich、Mark D. Distefano

  DOI：10.1039/c0cc03305g

  日期：——

  An aldehyde-containing alternative substrate for protein farnesyltransferase was prepared and shown to be enzymatically incorporated into a peptide and a protein. The protein was subsequently immobilized onto aminooxy-functionalized agarose beads or labeled with a fluorophore. This method for protein modification provides an alternative to the commonly employed Cu(I)-catalyzed click reaction.

  一种含醛的蛋白质法尼基转移酶替代底物已被制备，并显示出可以被酶学地结合到肽和蛋白质中。该蛋白随后被固定在氨氧基功能化的琼脂糖珠上，或者用荧光基团标记。此种蛋白质修饰方法提供了一种替代于常用的铜(I)催化的点击反应的新选择。
• Transition State Analysis of Model and Enzymatic Prenylation Reactions
  作者：Stepan Lenevich、Juhua Xu、Ayako Hosokawa、Christopher J. Cramer、Mark D. Distefano

  DOI：10.1021/ja069119j

  日期：2007.5.1

  substitution reactions with dimethylallyl chloride were first studied. 13C Kinetic isotope effects (KIEs) for the model reactions were measured by a natural abundance NMR method and used to validate the computational methods that would be used in the subsequent determination of the enzymatic TS structure. Using a primary 13C KIE and a secondary 2H KIE measured via mass spectrometry, a TS structure for the enzyme-catalyzed

  为了获得酶催化异戊二烯化反应的过渡态 (TS) 结构，首先研究了 SN1 和 SN2 模型与二甲基烯丙基氯的取代反应。模型反应的 13C 动力学同位素效应 (KIE) 通过天然丰度 NMR 方法进行测量，并用于验证将用于随后确定酶促 TS 结构的计算方法。使用通过质谱测量的初级 13C KIE 和次级 2H KIE，计算酶催化反应的 TS 结构；使用 mPW1N 泛函结合 6-31+G(d) 基组的电子结构理论的密度泛函水平用于这些计算。该结构的 CO 键长为 1.69 A，C-S 键长为 3.70 A。
• Synthesis, Properties, and Applications of Diazotrifluropropanoyl-Containing Photoactive Analogs of Farnesyl Diphosphate Containing Modified Linkages for Enhanced Stability
  作者：Marisa L. Hovlid、Rebecca L. Edelstein、Olivier Henry、Joshua Ochocki、Amanda DeGraw、Stepan Lenevich、Trista Talbot、Victor G. Young、Alan W. Hruza、Fernando Lopez-Gallego、Nicholas P. Labello、Corey L. Strickland、Claudia Schmidt-Dannert、Mark D. Distefano

  DOI：10.1111/j.1747-0285.2009.00914.x

  日期：2010.1

  Photoactive analogs of farnesyl diphosphate (FPP) are useful probes in studies of enzymes that employ this molecule as a substrate. Here, we describe the preparation and properties of two new FPP analogs that contain diazotrifluoropropanoyl photophores linked to geranyl diphosphate via amide or ester linkages. The amide‐linked analog (3) was synthesized in 32P‐labeled form from geraniol in seven steps

  法呢基二磷酸 (FPP) 的光活性类似物是研究使用该分子作为底物的酶的有用探针。在这里，我们描述了两种新的 FPP 类似物的制备和性质，它们包含通过酰胺或酯键连接到香叶基二磷酸的重氮三氟丙酰基光团。酰胺连接的类似物 ( 3 ) 以32 P 标记的形式从香叶醇中分七个步骤合成。用酿酒酵母蛋白法呢基转移酶 (ScPFTase) 进行的实验表明 3 是该酶的替代底物。[ 32]光解实验P]3 表明该化合物标记了法呢基转移酶和香叶基香叶基转移酶（1 型和 2 型）的 β 亚基。然而，酰胺连接的探针 3 在长期储存后会发生重排，变成不具有光化学反应性的异构三唑酮，因此使用不便。为了解决这个稳定性问题，从香叶醇中分六个步骤制备了酯连接的类似物4。计算分析和 X 射线晶体学研究表明，4以与 FPP 类似的方式与蛋白质法呢基转移酶 (PFTase) 结合。化合物4也是 PFTase 的替代底物，32 P 标记的形式选择性地光交联
• Farnesyl Diphosphate Analogues with ω-Bioorthogonal Azide and Alkyne Functional Groups for Protein Farnesyl Transferase-Catalyzed Ligation Reactions
  作者：Guillermo R. Labadie、Rajesh Viswanathan、C. Dale Poulter

  DOI：10.1021/jo7017747

  日期：2007.11.1

  [Graphics]Eleven farnesyl diphosphate analogues, which contained (omega-azide or alkyne substituents suitable for bioorthogonal Staudinger and Huisgen [3 + 2] cycloaddition coupling reactions, were synthesized. The analogues were evaluated as substrates for the alkylation of peptide cosubstrates by yeast protein farnesyl transferase. Five of the diphosphates were good alternative substrates for farnesyl diphosphate (FPP). Steady-state kinetic constants were measured for the active compounds, and the products were characterized by HPLC and LC-MS. Two of the analogues gave steady-state kinetic parameters (k(cat) and K-m) very similar to those of the natural substrate.