3-keto-5-aminohexanoate | 19355-90-9

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: 3-keto-5-aminohexanoate
• 英文别名: (5S)-5-ammonio-3-oxohexanoate；(5S)-5-azaniumyl-3-oxohexanoate
• CAS: 19355-90-9
• 化学式: C₆H₁₁NO₃
• 分子量: 145.158
• InChiKey: FAASBXNEOGMQHS-BYPYZUCNSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.2
• 重原子数：
  10
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  80.4
• 氢给体数：
  2
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-keto-5-aminohexanoate 、 (2R)-N-[3-(2-acetylsulfanylethylimino)-3-oxidopropyl]-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonatooxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl]oxy-2-hydroxy-3,3-dimethylbutanimidate 生成 L-3-aminobutyryl-CoA 、 acetoacetic acid anion
  参考文献：
  名称：

  Pathway of lysine degradation in Fusobacterium nucleatum

  摘要：

  Lysine被Fusobacterium nucleatum ATCC 25586发酵，形成约1摩尔的醋酸和丁酸。通过使用[1-14C]赖氨酸或[6-14C]赖氨酸，醋酸和丁酸被证明来自赖氨酸的两端，其中醋酸优先从碳原子1和2形成，而丁酸优先从碳原子3到6形成。这表明赖氨酸碳链在碳原子2和3以及碳原子4和5之间被切断，前者占主导地位。[1-14C]醋酸也被广泛地并入丁酸中，优先进入碳原子3和4。F. nucleatum的细胞提取物被证明能催化赖氨酸降解的3-酮，5-氨基己酸途径反应，该途径先前在降解赖氨酸的梭菌中已被描述。3-酮，5-氨基己酸裂解酶被部分纯化，并显示出与梭菌酶类似的性质。我们得出结论，赖氨酸降解的途径和酶在F. nucleatum和降解赖氨酸的梭菌中是相似的。

  DOI：

  10.1128/jb.152.1.201-207.1982
• 作为产物：
  描述：

  (3S,5S)-3,5-Diamino-hexansaeure 在 nicotinamide adenine dinucleotide phosphate 、 L-erythro-3,5-diaminohexanoate dehydrogenase from candidatus cloacamonas acidaminovorans 作用下， 以 aq. phosphate buffer 、 水 为溶剂， 生成 3-keto-5-aminohexanoate
  参考文献：
  名称：

  l-赤型-3,5-二氨基己酸脱氢酶的晶体结构和催化机理及β-氨基酸不对称合成的合理工程

  摘要：

  氨基酸脱氢酶 (AADH) 作为生物催化剂在手性氨基酸的不对称合成中显示出相当大的潜力。然而，与广泛研究的α-AADHs相比，关于能够合成β-氨基酸的β-AADHs的知识有限。在此，我们报告了l - erythro的晶体结构‐3,5-二氨基己酸脱氢酶及其变体，β-AADH 家族的唯一已知成员。晶体结构分析、定点诱变研究和量子化学计算揭示了 α-AADH 在底物结合和催化机制方面的差异。然后获得了许多合理设计的变体，对各种脂肪族 β-氨基酸的活性提高（110-800 倍），而没有对映选择性权衡。使用具有出色对映选择性 (>99% ee ) 和高分离产率 (86–87%)的出色变体制备了两种 β-氨基酸。这些结果为深入了解 3,5-DAHDH 的分子机制提供了重要见解，并为进一步设计用于 β-氨基酸不对称合成的 β-AADH 奠定了坚实的基础。

  DOI：

  10.1002/anie.202017225

文献信息

• Non-standard amino acid conjugates of amphetamine and processes for making and using the same
  申请人：Mickle Travis C.

  公开号：US20080139653A1

  公开（公告）日：2008-06-12

  Disclosed are amphetamine prodrug compositions comprising at least one non-standard amino acid conjugate of amphetamine, a salt thereof, a derivative thereof, or a combination thereof. Methods of making and using the same are also disclosed.

  揭示了包含至少一种苯丙胺非标准氨基酸共轭物、其盐、衍生物或其组合的苯丙胺前体组合物。还公开了制备和使用这些组合物的方法。
• Non-Standard Amino Acid Conjugates of Amphetamine and Processes for Making and Using the Same
  申请人：Mickle Travis C.

  公开号：US20090234018A1

  公开（公告）日：2009-09-17

  Disclosed are amphetamine prodrug compositions comprising at least one non-standard amino acid conjugate of amphetamine, a salt thereof, a derivative thereof, or a combination thereof. Methods of making and using the same are also disclosed.

  本发明涉及一种安非他命前药组合物，该组合物包含至少一种安非他命的非标准氨基酸结合物，其盐，衍生物或其组合物。本发明还公开了制备和使用该组合物的方法。
• Polar Hydrophilic Prodrugs and Non-Standard Amino Acid Conjugates of Amphetamine and Other Stimulants and Processes for Making and Using the Same
  申请人：Mickle Travis C.

  公开号：US20100292336A1

  公开（公告）日：2010-11-18

  Disclosed are polar, hydrophilic stimulant prodrug compositions comprising at least one stimulant chemically attached to a polar hydrophilic ligand, a salt thereof, a derivative thereof, or a combination thereof. Also disclosed are non-standard amino acid conjugates of amphetamine. Methods of making and using the same are also disclosed.

  公开了一种极性、亲水性兴奋剂前药组合物，包括至少一种兴奋剂化学连接到极性亲水性配体、其盐、其衍生物或其组合物。还公开了安非他命的非标准氨基酸共轭物。还公开了制备和使用它们的方法。
• 3-Keto-5-aminohexanoate Cleavage Enzyme
  作者：Marco Bellinzoni、Karine Bastard、Alain Perret、Anne Zaparucha、Nadia Perchat、Carine Vergne、Tristan Wagner、Raquel C. de Melo-Minardi、François Artiguenave、Georges N. Cohen、Jean Weissenbach、Marcel Salanoubat、Pedro M. Alzari

  DOI：10.1074/jbc.m111.253260

  日期：2011.8

  The exponential increase in genome sequencing output has led to the accumulation of thousands of predicted genes lacking a proper functional annotation. Among this mass of hypothetical proteins, enzymes catalyzing new reactions or using novel ways to catalyze already known reactions might still wait to be identified. Here, we provide a structural and biochemical characterization of the 3-keto-5-aminohexanoate cleavage enzyme (Kce), an enzymatic activity long known as being involved in the anaerobic fermentation of lysine but whose catalytic mechanism has remained elusive so far. Although the enzyme shows the ubiquitous triose phosphate isomerase (TIM) barrel fold and a Zn2+ cation reminiscent of metal-dependent class II aldolases, our results based on a combination of x-ray snapshots and molecular modeling point to an unprecedented mechanism that proceeds through deprotonation of the 3-keto-5-aminohexanoate substrate, nucleophilic addition onto an incoming acetyl-CoA, intramolecular transfer of the CoA moiety, and final retro-Claisen reaction leading to acetoacetate and 3-aminobutyryl-CoA. This model also accounts for earlier observations showing the origin of carbon atoms in the products, as well as the absence of detection of any covalent acyl-enzyme intermediate. Kce is the first representative of a large family of prokaryotic hypothetical proteins, currently annotated as the "domain of unknown function" DUF849.
• Baker J.J.; Jeng I.; Barker H.A., J Biol Chem, 1972, 0021-9258, 7724-34
  作者：Baker J.J.、Jeng I.、Barker H.A.

  DOI：——

  日期：——