Pressinoic acid

• 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: Pressinoic acid
• 英文别名: H-Cys(1)-Tyr-Phe-Gln-Asn-Cys(1)-al；3-[(4R,7S,10S,13S,16S,19R)-19-amino-7-(2-amino-2-oxoethyl)-13-benzyl-4-formyl-16-[(4-hydroxyphenyl)methyl]-6,9,12,15,18-pentaoxo-1,2-dithia-5,8,11,14,17-pentazacycloicos-10-yl]propanamide
• 化学式: C₃₃H₄₂N₈O₉S₂
• 分子量: 758.877
• InChiKey: CCXKETUXPGPZMQ-IWGFAJNXSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.2
• 重原子数：
  52
• 可旋转键数：
  10
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.39
• 拓扑面积：
  346
• 氢给体数：
  9
• 氢受体数：
  12

反应信息

• 作为反应物：
  描述：

  谷胱甘肽 、 Pressinoic acid 在 potassium chloride 作用下， 以 水 为溶剂， 生成 L-谷胱甘肽 (氧化型) 、
  参考文献：
  名称：

  Kinetics and Equilibria of the Formation and Reduction of the Disulfide Bonds in Arginine-Vasopressin and Oxytocin by Thiol/Disulfide Interchange with Glutathione and Cysteine

  摘要：

  Rate and equilibrium constants are reported for reduction of the disulfide bonds in the neurohypophyseal peptide hormones oxytocin (OT) and arginine-vasopressin (AVP) by thiol/disulfide interchange with glutathione (GSH) and cysteine (CySH) and for formation of the disulfide bonds by thiol/disulfide interchange with oxidized glutathione (GSSG) and cystine (CySSCy). The reactions take place in two steps. In the first step of the reduction reactions, AVP and OT react with GSH and CySH to form peptide-GSH and peptide-CySH mixed disulfides, which in turn react with another molecule of GSH or CySH to give the reduced dithiol form of the peptide and GSSG or CySSCy. Analysis of the forward and reverse rate constants indicates that which step is rate determining depends on the concentration of GSH or CySH. At physiological concentrations of GSH and CySH, intramolecular thiol/disulfide interchange in the mixed disulfides to reform the native disulfide bonds is faster than reaction with another molecule of GSH or CySH, even though intramolecular thiol/disulfide interchange involves closure of 20-membered rings. Rate constants for reaction of GSH and CySH with the disulfide bonds of AVP and OT are 1-2 orders of magnitude larger than for reaction with disulfide bonds formed by two cysteine-containing peptides, which suggests that the disulfide bonds in the neurohypophyseal peptide hormones are strained. Equilibrium constants are also reported for reaction of GSH with the hexapeptide analogs of AVP and OT, pressinoic acid (PA), and tocinoic acid (TA). A reduction potential of -0.216 V was calculated for the disulfide bonds of OT and TA from the thiol/disulfide interchange equilibrium constants. Reduction potentials of -0.229 V and -0.227 V were calculated for the disulfide bonds in AVP and PA, respectively. The similarity of the reduction potentials for OT and TA and for AVP and PA indicates that the acyclic tripeptide tails of OT and AVP have little affect on the redox properties of their disulfide bonds.

  DOI：

  10.1021/jo00094a039

文献信息

• Kinetics and Equilibria of the Formation and Reduction of the Disulfide Bonds in Arginine-Vasopressin and Oxytocin by Thiol/Disulfide Interchange with Glutathione and Cysteine
  作者：Dallas L. Rabenstein、Pauline L. Yeo

  DOI：10.1021/jo00094a039

  日期：1994.7

  Rate and equilibrium constants are reported for reduction of the disulfide bonds in the neurohypophyseal peptide hormones oxytocin (OT) and arginine-vasopressin (AVP) by thiol/disulfide interchange with glutathione (GSH) and cysteine (CySH) and for formation of the disulfide bonds by thiol/disulfide interchange with oxidized glutathione (GSSG) and cystine (CySSCy). The reactions take place in two steps. In the first step of the reduction reactions, AVP and OT react with GSH and CySH to form peptide-GSH and peptide-CySH mixed disulfides, which in turn react with another molecule of GSH or CySH to give the reduced dithiol form of the peptide and GSSG or CySSCy. Analysis of the forward and reverse rate constants indicates that which step is rate determining depends on the concentration of GSH or CySH. At physiological concentrations of GSH and CySH, intramolecular thiol/disulfide interchange in the mixed disulfides to reform the native disulfide bonds is faster than reaction with another molecule of GSH or CySH, even though intramolecular thiol/disulfide interchange involves closure of 20-membered rings. Rate constants for reaction of GSH and CySH with the disulfide bonds of AVP and OT are 1-2 orders of magnitude larger than for reaction with disulfide bonds formed by two cysteine-containing peptides, which suggests that the disulfide bonds in the neurohypophyseal peptide hormones are strained. Equilibrium constants are also reported for reaction of GSH with the hexapeptide analogs of AVP and OT, pressinoic acid (PA), and tocinoic acid (TA). A reduction potential of -0.216 V was calculated for the disulfide bonds of OT and TA from the thiol/disulfide interchange equilibrium constants. Reduction potentials of -0.229 V and -0.227 V were calculated for the disulfide bonds in AVP and PA, respectively. The similarity of the reduction potentials for OT and TA and for AVP and PA indicates that the acyclic tripeptide tails of OT and AVP have little affect on the redox properties of their disulfide bonds.