-enkephalyl-arg⁶-phe⁷ | 73024-95-0

• 物质功能分类: 生物化工 - 多肽
• 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: -enkephalyl-arg⁶-phe⁷
• 英文别名: [Met⁵]-enkephalin-Arg⁶-Phe⁷；Met-enkephalin-Arg-Phe；met-enkephalin-RF-OH；M-Enk-RF；Tyr-Gly-Gly-Phe-Met-Arg-Phe；Met-enk-RF；(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-(diaminomethylideneamino)pentanoyl]amino]-3-phenylpropanoic acid
• CAS: 73024-95-0
• 化学式: C₄₂H₅₆N₁₀O₉S
• mdl: MFCD00076425
• 分子量: 877.034
• InChiKey: KTQKWSPZOZKAEE-LJADHVKFSA-N

物化性质

• 密度：
  1.38±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.9
• 重原子数：
  62
• 可旋转键数：
  26
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.38
• 拓扑面积：
  348
• 氢给体数：
  11
• 氢受体数：
  12

制备方法与用途

Met-Enkephalin Arg-Phe 是一种含有镇痛作用的天然七肽[1]。

反应信息

• 作为反应物：
  描述：

  -enkephalyl-arg⁶-phe⁷ 在 angiotensin I converting enzyme 作用下， 以 various solvent(s) 为溶剂， 生成 L-arginyl-L-phenylalanine 、 蛋氨酸-脑啡呔
  参考文献：
  名称：

  Differences in the hydrolysis of enkephalin congeners by the two domains of angiotensin converting enzyme

  摘要：

  The hydrolysis of enkephalin (Enk) congeners by the isolated N- (N-ACE) and C-domain of angiotensin I converting enzyme (ACE) and by the two-domain somatic ACE was investigated. Both Leu(5)- and Met(5)-Enk were cleaved faster by the C-domain than by N-ACE; rates with somatic ACE were 1600 and 2500 nmol/min/nmol enzyme with both active sites being involved. Substitution of Gly(2) by D-Ala(2) reduced the rate to 1/3rd to 1/7th of that of the Enks. N-ACE cleaved Met(5)-Enk-Arg(6)-Phe(7) faster than the C-domain, probably with the highest turnover number of any naturally occurring ACE substrate (7600 min(-1)). This heptapeptide is also hydrolyzed in the absence of Cl-, but the activation by Cl- is unique; Cl- enhances the hydrolysis of the heptapeptide by N-ACE but inhibits it by the C-domain, yielding about a 5 fold difference in the turnover number at physiological pH. This difference may result in the predominant role of the N-domain in converting Met(5)-Enk-Arg(6)-Phe(7) to Enk in vivo. (C) 1997 Elsevier Science Inc.

  DOI：

  10.1016/s0006-2952(97)00087-7

文献信息

• Effects of three peptidase inhibitors, amastatin, captopril and phosphoramidon, on the hydrolysis of [Met5]-enkephalin-Arg6-Phe7 and other opioid peptides
  作者：Toyokazu Hiranuma、K. Kitamura、Takao Taniguchi、Tomomi Kobayashi、Raita Tamaki、Masayuki Kanai、Kazuhito Akahori、Kayoko Iwao、T. Oka

  DOI：10.1007/pl00005168

  日期：1998.3.10

  The contents of [Met(5)]-enkephalin-Arg(6)-Phe(7) (met-enk-RF) and its six hydrolysis products: Y, YG, YGG, YGGE YGGFM, and YGGFMR were estimated after incubating met-enk-RF with either a guinea-pig ileal or striatal membrane fraction for various times at 37 degrees C, After 45 min incubation with either ileal or striatal membranes, met-enk-RF was completely hydrolyzed, yielding Y as the major product. Incubation with either membrane preparation for 60 min in the presence of the aminopeptidase inhibitor amastatin hydrolyzed 90 or 92% of met-enk-RF, respectively, with YGG being the major product. If the dipeptidyl carboxypeptidase I inhibitor captopril is also included in the incubation, met-enk-RF hydrolysis decreases by about half for both membranes, with YGG remaining the major product. Inclusion of three peptidase inhibitors, amastatin, captopril, and phosphoramidon (inhibition of endopeptidase-24.11) further reduced met-enk-hydrolysis, with 87% or more remaining intact. This shows that met-enk-RF was mainly hydrolyzed by three enzymes, amastatin-sensitive aminopeptidase, captopril-sensitive dipeptidyl carboxypeptidase I and phosphoramidon-sensitive endopeptidase-24.11, in both ileal and striatal membranes.Additionally, estimations of [Leu(5)]-enkephalin (leu-enk), alpha- and beta-neoendorphins (alpha- and beta-neoends), and dynorphin B (dyn B) contents after incubating the individual peptides with striatal membrane for 60 min in the presence of the three peptidase inhibitors showed that 98, 32, 5, and 23%, respectively, remained intact.Our previous studies together with the data obtained here show that one group of endogenous opioid peptides: met-enk, leu-enk, met-enk-RF, met-enk-RGL, and dyn A-(1-8) are largely or almost exclusively hydrolyzed by the three enzymes, amastatin-sensitive aminopeptidase, captopril-sensitive dipeptidyl carboxypeptidase I, and phoramidon-sensitive endopeptidase-4.11, and indicate that an unidentified fourth enzyme(s) is involved in the hydrolysis of another group of peptides: alpha-neoend, beta-neoend, and dyn B.