N-benzyloxycarbonyl-L-asparatic acid diallyl ester | 127949-86-4

• 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: N-benzyloxycarbonyl-L-asparatic acid diallyl ester
• 英文别名: N-Cbz-L-aspartic acid diallyl ester；Cbz-Asp(OAll)-OAll；bis(prop-2-enyl) (2S)-2-(phenylmethoxycarbonylamino)butanedioate
• CAS: 127949-86-4
• 化学式: C₁₈H₂₁NO₆
• 分子量: 347.368
• InChiKey: DDHAPMJBVMDOHM-HNNXBMFYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  2.5
• 重原子数：
  25
• 可旋转键数：
  13
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.28
• 拓扑面积：
  90.9
• 氢给体数：
  1
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  N-benzyloxycarbonyl-L-asparatic acid diallyl ester 在 sodium hydroxide 、 mercaptoethyl alcohol 作用下， 以 乙醇 、 水 、 甘油 、 乙腈 为溶剂， 反应 14.0h， 生成
  参考文献：
  名称：

  Enzymic Synthesis of the Delicious Peptide Fragments in Eutectic Mixtures

  摘要：

  The feasibility of flavor peptide production has been investigated using proteases in liquid/semiliquid eutectic mixtures comprised of the substrates together with small amounts of water and alcohols (19-24% w/w). The three functional fragments of the so-called ''Delicious Octapeptide'', L-Lys-Gly, L-Asp-Glu-Glu, and L-Ser-Leu-Ala, were obtained in good yields without any requirement for the regioselective side-chain protection of multifunctional amino acids. The peptides were synthesized on a preparative scale in overall yields of 29-77% and were fully characterized.

  DOI：

  10.1021/jf00057a040
• 作为产物：
  描述：

  N-CBZ-L-天冬氨酸 、 烯丙醇 在 N-羟基-7-氮杂苯并三氮唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 N,N-二异丙基乙胺 作用下， 以 二氯甲烷 为溶剂， 反应 24.0h， 生成 N-benzyloxycarbonyl-L-asparatic acid diallyl ester
  参考文献：
  名称：

  A versatile and selective chemo-enzymatic synthesis of β-protected aspartic and γ-protected glutamic acid derivatives

  摘要：

  Two versatile, high yielding, and efficient chemo-enzymatic methods for the synthesis of beta-protected Asp and gamma-protected Glu derivatives using Alcalase are described. The first method is based on the alpha-selective enzymatic hydrolysis of symmetrical aspartyl and glutamyl diesters. The second method involving mixed diesters comprises a three-step protocol using (i) alpha-selective enzymatic methyl-esterification, (ii) chemical beta-esterification, and finally (iii) alpha-selective enzymatic methyl ester hydrolysis. The yields of the purified beta- and gamma-esters range from 77% to 91%. (C) 2009 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2009.03.130

文献信息

• New enzymatic approach to the synthesis of convenient aspartic acid intermediates in peptide chemistry. Synthesis of n-benzyloxycarbonyl-l-aspartic acid β-allyl ester.
  作者：N. Xaus、P. Clapés、E. Bardají、J.L. Torres、X. Jorba、J. Mata、G. Valencia

  DOI：10.1016/s0040-4020(01)89204-8

  日期：1989.1

  Aspartic acid side chain protection by allyl ester functions has been facilitated by the direct synthesis of Z-Asp(OA11)-OH which can be performed by selective hydrolysis of Z-Asp(OA11)-OA11 by means of papain catalysis. Both an optimization study and a batch synthesis are reported. Other synthetic routes are discussed.

  Z-Asp（OA11）-OH的直接合成促进了烯丙基酯功能对天冬氨酸侧链的保护，这可以通过木瓜蛋白酶催化选择性水解Z-Asp（OA11）-OA11来进行。既有优化研究，也有批次综合报告。讨论了其他合成路线。
• 3,5-disubstituted 4,5-dihydroisoxazoles as transglutaminase inhibitors
  申请人：SYNTEX (U.S.A.) INC.

  公开号：EP0237082B1

  公开（公告）日：1991-05-29
• Engineering Subtilisin for Peptide Coupling: Studies on the Effects of Counterions and Site-Specific Modifications on the Stability and Specificity of the Enzyme
  作者：Pamela Sears、Matthias Schuster、Peng Wang、Krista Witte、Chi-Huey Wong

  DOI：10.1021/ja00094a005

  日期：1994.7

  Several variants derived from the thermostable subtilisin 8397 were made in order to create an enzyme that is more stable toward organic solvents or has a broader specificity for the P-1' residue in amidation or is more effective for peptide segment ligation in aqueous solution. To improve the stability in organic solvents, one of three surface charges was removed each time from 8397 to create the variants: Lys43 --> Asn (K43N), Lys256 --> Tyr (K256Y), and Asp181 --> Asn (D181N). Although the stabilities of these variants in high concentrations of hydrophilic organic solvents were higher than that of the wild-type enzyme, the D181N variant was less stable than the 8397 variant. It appears that removal of isolated surface charges does not necessarily improve the enzyme stability in polar organic solvents. A dramatic change of the enzyme stability in dimethylformamide (DMF) was, however, observed in the presence of different counterions. Subtilisin BPN' lyophilized from Tris-HCl buffer (50 mM, pH 8.4) and suspended in DMF (solid partially soluble), for example, was completely inactivated in 30 min at 25 degrees C, while the enzyme still retained about 70% of the original activity in a week if lyophilized from sodium phosphate buffer (50 mM, pH 8.4) (solid completely insoluble in DMF). In general, the enzyme lyophilized from organic buffers deactivates in DMF much faster than that from inorganic buffers. A similar counterion effect was observed with other variants. These studies suggest that subtilisins are very unstable when exposed directly to DMF; the stability is, however, markedly improved if the enzyme is protected by water or salts from contact with the solvent. To use subtilisins and variants in transesterification or aminolysis in organic solvents, water (3-30%) is usually present in order to have significant reactivity, and for transesterifications, it was found that a good rate and yield could be achieved in ethanol containing 30% water. For use in peptide segment ligation in aqueous solution, the active-site serine of subtilisin 8397/C206Q was converted chemically to cysteine, forming thiosubtilisin 8397/C206Q, and the aminolysis:hydrolysis ratio was found to be several orders of magnitude higher than that for subtilisin BPN' and comparable to that for thiosubtilisin BPN'. The 8397 variant was also modified at the S-1' site via M222A/Y217W mutations to broaden the P-1' specificity.
• XAUS, N.;CLAPES, P.;BARDAJI, E.;TORRES, J. L.;JORBA, X.;MATA, J.;VALENCIA+, TETRAHEDRON, 45,(1989) N3, C. 7421-7426
  作者：XAUS, N.、CLAPES, P.、BARDAJI, E.、TORRES, J. L.、JORBA, X.、MATA, J.、VALENCIA+

  DOI：——

  日期：——
• US4912120A
  申请人：——

  公开号：US4912120A

  公开（公告）日：1990-03-27