(R)-1-aminopropan-2-ol

• 分子结构分类: 有机化合物 - 有机氮化合物
• 英文名称: (R)-1-aminopropan-2-ol
• 英文别名: 2-Hydroxy-propyl-ammonium；[(2R)-2-hydroxypropyl]azanium
• 化学式: C₃H₉NO*H
• 分子量: 76.1185
• InChiKey: HXKKHQJGJAFBHI-GSVOUGTGSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  -1
• 重原子数：
  5
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  1.0
• 拓扑面积：
  47.9
• 氢给体数：
  2
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  dimethyl 3-methoxy-4-oxo-1-[(1S)-2-oxocyclopentyl]pyridine-2,5-dicarboxylate 、 (R)-1-aminopropan-2-ol 在 potassium carbonate 、 溶剂黄146 作用下， 以 乙腈 为溶剂， 反应 16.0h， 生成 methyl (2S,6S,8R)-13-methoxy-8-methyl-11,14-dioxo-7-oxa-1,10-diazatetracyclo[10.4.0.02,6.06,10]hexadeca-12,15-diene-15-carboxylate
  参考文献：
  名称：

  POLYCYCLIC-CARBAMOYLPYRIDONE COMPOUNDS AND THEIR PHARMACEUTICAL USE

  摘要：

  揭示了用于治疗人类免疫缺陷病毒（HIV）感染的化合物。这些化合物具有以下的化学式（Ia）：包括立体异构体和其药用可接受的盐，其中A、A′、R1和R2如本文所定义。还揭示了与制备和使用这些化合物相关的方法，以及包含这些化合物的药物组合物。

  公开号：

  US20160289246A1
• 作为产物：
  描述：

  adenosylcob(III)inamide 、 水 生成 (R)-1-aminopropan-2-ol 、 adenosylcob(III)yrate
  参考文献：
  名称：

  CbiZ, an amidohydrolase enzyme required for salvaging the coenzyme B ₁₂ precursor cobinamide in archaea

  摘要：

  通过遗传和生化手段，确定了从环境中回收辅酶B12前体二氰基钴胺（Cbi）的途径的存在。该途径需要一个以前未被识别的酰胺水解酶酶的功能，将腺苷基钴胺转化为腺苷基钴酸，这是新生辅酶B12生物合成途径的一个真正中间体。克隆了甲烷生成古菌Methanosarcina mazei Göl菌株的cbiZ基因，过量表达在大肠杆菌中，并分离纯化了重组蛋白。HPLC，UV-可见光谱，MS和生物测定数据确定了腺苷基钴酸作为CbiZ催化反应的协因子产物。在极端嗜盐古菌Halobacterium sp. NRC-1菌株中失活cbiZ基因会阻止该古菌回收Cbi。在被阻断了Cbi回收途径的细菌Salmonella enterica中，cbiZ功能恢复了Cbi回收。通过CbiZ酶回收Cbi似乎是一种古菌策略，因为所有产生B12的古菌基因组都有一个cbiZ同源基因。讨论了原核生物中演化出两种不同的Cbi回收途径的原因。

  DOI：

  10.1073/pnas.0305939101

文献信息

• The biosynthesis of adenosylcobalamin (vitamin B12)
  作者：Martin J. Warren、Evelyne Raux、Heidi L. Schubert、Jorge C. Escalante-Semerena

  DOI：10.1039/b108967f

  日期：2002.7.18

  Vitamin B12, or cobalamin, is one of the most structurally complex small molecules made in Nature. Major progress has been made over the past decade in understanding how this synthesis is accomplished. This review covers some of the most important findings that have been made and provides the reader with a complete description of the transformation of uroporphyrinogen III into adenosylcobalamin (AdoCbl)

  维生素B12或钴胺素是自然界中结构最复杂的小分子之一。在过去的十年中，在理解如何完成这种合成方面取得了重大进展。这篇综述涵盖了一些最重要的发现，并为读者提供了将尿卟啉原原III转化为腺苷钴胺素（AdoCbl）的完整说明。引用了183篇参考文献。
• Microbial metabolism of amino ketones. <scp>l</scp>-1-aminopropan-2-ol dehydrogenase and <scp>l</scp>-threonine dehydrogenase in <i>Escherichia coli</i>
  作者：JM Turner

  DOI：10.1042/bj1040112

  日期：1967.7.1

  intermediary metabolites and substrate analogues have no effect on the oxidation of dl-1-aminopropan-2-ol to aminoacetone by washed-cell suspensions of Escherichia coli. Only dl-2-hydroxy-2-phenylethylamine, dl-1,3-diaminopropan-2-ol, dl-serine and l-1-(3,4-dihydroxyphenyl)-2-aminoethanol act as inhibitors. 2. Dialysed cell-free extracts of E. coli exhibit an NAD(+)-dependent dl-1-aminopropan-2-ol-dehydrogenase

  1.多种中间产物和底物类似物对大肠杆菌洗涤过的细胞悬浮液将dl-1-氨基丙烷-2-醇氧化为氨基丙酮没有影响。仅dl-2-羟基-2-苯基乙胺，dl-1,3-二氨基丙烷-2-醇，dl-丝氨酸和l-1-（3,4-二羟基苯基）-2-氨基乙醇用作抑制剂。透析后的大肠杆菌无细胞提取物显示出约NAD（+）依赖性的dl-1-氨基丙烷-2-醇-脱氢酶活性。形成8摩尔氨基丙酮/毫克。蛋白质/分钟 在最佳pH值下 10.辅酶和dl-氨基醇的K（m）值约为10。分别为0.4和10.0mm。在pH7.0-7.2时出现较小的活性峰，在pH7时NAD（+）的K（m）约为10。0.05毫米 3. dl-2-羟基-2-苯乙胺，dl-1-氨基丙烷-2抑制无细胞提取物中的酶活性，3-二醇和dl-丝氨酸。dl-苯基丝氨酸和dl-1-氨基丁烷-2-醇被氧化为以氨基酮形式反应的化合物。4.在新鲜的无细胞提取物中，l（+）-1-氨基丙
• Formation of Dg-1-amino-2-propanol by a highly purified enzyme from Escherichia coli
  作者：Eugene E. Dekker、Richard R. Swain

  DOI：10.1016/0304-4165(68)90150-5

  日期：1968.5
• Microbial metabolism of amino ketones. Aminoacetone formation from 1-aminopropan-2-ol by a dehydrogenase in <i>escherichia coli</i>
  作者：JM Turner

  DOI：10.1042/bj0990427

  日期：1966.5.1

  1. Washed-cell suspensions of Escherichia coli, incubated at the optimum pH of 6.4 and with a saturating substrate concentration of approx. 10mm, convert dl-1-aminopropan-2-ol into aminoacetone at a rate of approx. 4.0mmumoles/mg. dry wt. of cells/min. at 30 degrees . 2. Mg(2+), Mn(2+), Co(2+), Zn(2+), Ca(2+), K(+) and NH(4) (+), as sulphates, and EDTA have no effect on this rate, although Cu(2+) inhibits and Fe(2+) activates to some extent. 3. Conditions of growth markedly affect the rate of aminoacetone production by cell suspensions. 4. Dialysed cell-free extracts of E. coli exhibit 1-aminopropan-2-ol-dehydrogenase activity, the enzyme having optimum activity at pH7.0, a requirement for NAD(+) and K(+), and a K(m) for the amino alcohol substrate of 0.8mm, calculated for a single enantiomorph. 5. Under optimum conditions 1-aminopropan-2-ol dehydrogenase forms aminoacetone at rate of approx. 3.0mmumoles/mg. of protein/min. at 37 degrees . The enzyme is only slightly inhibited by dl-3-hydroxybutyrate and dl-2-hydroxy-2-phenylethyl-amine. 6. l-Threonine-dehydrogenase activity is exhibited by both whole cells and cell-free extracts. Whole cells produce aminoacetone from l-threonine more slowly than they do from dl-1-aminopropan-2-ol, whereas the situation is reversed in cell-free extracts. Both kinetic evidence, and the fact that synthesis of 1-aminopropan-2-ol dehydrogenase, but not of threonine dehydrogenase, is repressed by compounds such as glucose and pyruvate, provide evidence that the amino alcohol is oxidized by a specific enyme. 7. The metabolic role of 1-aminopropan-2-ol dehydrogenase is discussed.
• Three-Dimensional Structure of the <scp>l</scp>-Threonine-<i>O</i>-3-phosphate Decarboxylase (CobD) Enzyme from <i>Salmonella enterica</i>^,
  作者：Cheom-Gil Cheong、Cary B. Bauer、Kevin R. Brushaber、Jorge C. Escalante-Semerena、Ivan Rayment

  DOI：10.1021/bi012111w

  日期：2002.4.1

  The three-dimensional structure of the pyridoxal 5'-phosphate (PLP)-dependent L-threonine-O-3-phosphate decarboxylase (CobD) from Salmonella enterica is described here. This enzyme is responsible for synthesizing (R)-1-amino-2-propanol phosphate which is the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin. The molecule is a molecular dimer where each subunit consists of a large and small domain. Overall the protein is very similar to the members of the family of aspartate aminotransferases. Indeed, the arrangement of the ligands surrounding the cofactor and putative substrate binding site are remarkably close to that observed in histidinol phosphate aminotransferase, which suggests that this latter enzyme might have been its progenitor. The only significant differences in structure occur at the N-terminus, which is approximately 12 residues shorter in CobD and does not form the same type of interdomain interaction common to other aminotransferases. CobD is unusual since within the aspartate aminotransferase subfamily of PLP-dependent enzymes the chemical transformations are substantially conserved, where the only exceptions are 1-aminocyclopropane-1-carboxylate synthase and CobD. Although there are a large number of PLP-dependent amino acid decarboxylases, these are generally larger and structurally distinct from the members of the aspartate aminotransferase subfamily of enzymes. The structure of CobD suggests that the chemical fate of the external aldimine can be redirected by modifications at the N-terminus of the protein. This study provides insight into the evolutionary history of the cobalamin biosynthetic pathway and raises the question of why most PLP-dependent decarboxylases are considerably larger enzymes.