(R)-β-bromo-isobutyric acid | 89361-97-7

• 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: (R)-β-bromo-isobutyric acid
• 英文别名: (R)-β-Brom-isobuttersaeure；(R)-3-Bromo-2-methylpropanoic acid；(2R)-3-bromo-2-methylpropanoic acid
• CAS: 89361-97-7
• 化学式: C₄H₇BrO₂
• 分子量: 167.002
• InChiKey: BUPXDXGYFXDDAA-VKHMYHEASA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.1
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  37.3
• 氢给体数：
  1
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (R)-β-bromo-isobutyric acid 、 氯甲酸异丁酯 在 N-甲基吗啉 作用下， 以 四氢呋喃 为溶剂， 反应 0.25h， 生成
  参考文献：
  名称：

  Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme

  摘要：

  我们合成了一般结构为 X-Lys-PO2H-Gly-Ala 的伪三肽和四肽氨基烷基膦酸，作为 D-Ala-D-Ala 添加酶的过渡态类似物。组装 C 端二肽单元的关键合成步骤是改良的阿勃梭夫反应，将溴丙酰基-D-丙氨酸甲酯与硅烷化的氨基烷基膦酸盐偶联。用纯化的大肠杆菌酶进行动力学测定发现，膦酸盐类似物是可逆的竞争性抑制剂，Ki 值在 200-700 µ>M> 之间。模仿 UDPMurNAc-L-Ala-γ-D-Glu-m-DAP 底物肽链的扩展类似物显示出与酶活性位点更强的结合亲和力。这是首次报道的 D-Ala-D-Ala 添加酶抑制剂。

  DOI：

  10.1039/a704097k
• 作为产物：
  描述：

  (R)-(+)-3-溴异丁酸甲酯 在 三丁基氧化锡 作用下， 以 甲苯 为溶剂， 反应 48.0h， 以60%的产率得到(R)-β-bromo-isobutyric acid
  参考文献：
  名称：

  Scope and Mechanism of Deprotection of Carboxylic Esters by Bis(tributyltin) Oxide

  摘要：

  Methyl and ethyl esters of aliphatic and aromatic carboxylic acids as well as benzyl carboxylates, thiol esters and double esters such as (pivaloyloxy)methyl carboxylates have been successfully cleaved with bis(tributyltin) oxide to give the free carboxylic acids in good yields. The reaction is carried out in aprotic solvents under essentially neutral conditions and thus this method can serve as an ideal procedure for the cleavages of esters with other functional groups and/or protecting groups acid and/or base sensitive. We demonstrated that the reaction displays a high level of chemoselectivity between methyl and ethyl esters versus tert-butyl esters and gamma-lactones. Bis(tributyltin) oxide is also a highly efficient reagent for the cleavage of acetates of primary and secondary alcohols and phenols. The limitations we found in the use of this reagent include the lack. of cleavage of esters sterically hindered around the carboxyl carbon and the carbinol group (i.e., esters of tertiary alcohols) and in carboxylic esters that contain a fluoroalkyl substituent. A resonable mechanistic explanation is discussed to account for the reaction pathway of the acyloxygen cleavage of(-)-(1R)-menthyl acetate.

  DOI：

  10.1021/jo00103a016

文献信息

• Mapping the substrate selectivity of new hydrolases using colorimetric screening: lipases from Bacillus thermocatenulatus and Ophiostoma piliferum, esterases from Pseudomonas fluorescens and Streptomyces diastatochromogenes
  作者：Andrew Man Fai Liu、Neil A Somers、Romas J Kazlauskas、Terry S Brush、Frank Zocher、Markus M Enzelberger、Uwe T Bornscheuer、Geoff P Horsman、Alessandra Mezzetti、Claudia Schmidt-Dannert、Rolf D Schmid

  DOI：10.1016/s0957-4166(01)00072-6

  日期：2001.3

  screened a general library of 29 substrates and a chiral library of 23 pairs of enantiomers. All four hydrolases catalysed the hydrolysis of unnatural substrates, but the two lipases accepted a broader range of substrates than the two esterases. As expected, the two lipases favoured more hydrophobic substrates, while the two esterases showed a preference for smaller substrates. Several moderately enantioselective

  生物化学和分子生物学的最新进展简化了新型水解酶的发现和制备。尽管这些水解酶可能解决了有机合成中的问题，但测量其选择性（尤其是对映选择性）仍然繁琐且耗时。最近，我们开发了一种比色筛选方法来测量水解酶的对映选择性。在这里，我们应用这种快速筛选方法来绘制四种新型水解酶的底物选择性图：来自嗜热芽孢杆菌的脂肪酶（DSM 730，BTL2）和丝状真菌Ophiostoma piliferum（NRRL 18917，OPL）以及来自两种细菌荧光假单胞菌（Pseudomonas fluorescens（ SIK-W1，酯酶I，PFE）和链霉菌（Tü20，SDE）。我们筛选了29种底物的通用文库和23对对映异构体的手性文库。所有四种水解酶均催化非天然底物的水解，但是与两种酯酶相比，两种脂肪酶接受的底物范围更广。不出所料，这两种脂肪酶偏爱疏水性更高的底物，而两种酯酶则偏爱较小的底物。确认了该酚醛酸酯的一些中等对映选择性反应：BTL2，丁酸酯，E
• Staellberg, Arkiv foer Kemi, 1958, vol. 12, p. 95,96
  作者：Staellberg

  DOI：——

  日期：——
• Staellberg, Arkiv foer Kemi, 1958, vol. 12, p. 131,133
  作者：Staellberg

  DOI：——

  日期：——
• Scope and Mechanism of Deprotection of Carboxylic Esters by Bis(tributyltin) Oxide
  作者：Claudio J. Salomon、Ernesto G. Mata、Oreste A. Mascaretti

  DOI：10.1021/jo00103a016

  日期：1994.12

  Methyl and ethyl esters of aliphatic and aromatic carboxylic acids as well as benzyl carboxylates, thiol esters and double esters such as (pivaloyloxy)methyl carboxylates have been successfully cleaved with bis(tributyltin) oxide to give the free carboxylic acids in good yields. The reaction is carried out in aprotic solvents under essentially neutral conditions and thus this method can serve as an ideal procedure for the cleavages of esters with other functional groups and/or protecting groups acid and/or base sensitive. We demonstrated that the reaction displays a high level of chemoselectivity between methyl and ethyl esters versus tert-butyl esters and gamma-lactones. Bis(tributyltin) oxide is also a highly efficient reagent for the cleavage of acetates of primary and secondary alcohols and phenols. The limitations we found in the use of this reagent include the lack. of cleavage of esters sterically hindered around the carboxyl carbon and the carbinol group (i.e., esters of tertiary alcohols) and in carboxylic esters that contain a fluoroalkyl substituent. A resonable mechanistic explanation is discussed to account for the reaction pathway of the acyloxygen cleavage of(-)-(1R)-menthyl acetate.
• Aminoalkylphosphinate inhibitors of D-Ala-D-Ala adding enzyme
  作者：David J. Miller、Stephen M. Hammond、Daniela Anderluzzi、Timothy D. H. Bugg

  DOI：10.1039/a704097k

  日期：——

  Pseudo-tri- and -tetra-peptide aminoalkylphosphinic acids of general structure X-Lys-PO2H-Gly-Ala have been synthesised as transition state analogues for D-Ala-D-Ala adding enzyme. The key synthetic step used to assemble the C-terminal dipeptide unit is a modified Arbusov reaction, coupling bromopropionyl-D-alanine methyl ester to a silylated aminoalkylphosphonite. Kinetic assays with the purified E. coli enzyme reveal that the phosphinate analogues act as reversible competitive inhibitors, with Ki values in the range 200–700 µ>M>. Extended analogues mimicking the peptide chain of the UDPMurNAc-L-Ala-γ-D-Glu-m-DAP substrate show increased binding affinity for the enzyme active site. These are the first reported inhibitors for D-Ala-D-Ala adding enzyme.

  我们合成了一般结构为 X-Lys-PO2H-Gly-Ala 的伪三肽和四肽氨基烷基膦酸，作为 D-Ala-D-Ala 添加酶的过渡态类似物。组装 C 端二肽单元的关键合成步骤是改良的阿勃梭夫反应，将溴丙酰基-D-丙氨酸甲酯与硅烷化的氨基烷基膦酸盐偶联。用纯化的大肠杆菌酶进行动力学测定发现，膦酸盐类似物是可逆的竞争性抑制剂，Ki 值在 200-700 µ>M> 之间。模仿 UDPMurNAc-L-Ala-γ-D-Glu-m-DAP 底物肽链的扩展类似物显示出与酶活性位点更强的结合亲和力。这是首次报道的 D-Ala-D-Ala 添加酶抑制剂。