O-乙酰基-L-高丝氨酸 | 7540-67-2

• 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
• 中文名称: O-乙酰基-L-高丝氨酸
• 中文别名: O-乙酰-L-丝氨酸盐酸盐；O-乙酰氧基-L-高丝氨酸
• 英文名称: O-acetyl-L-homoserine
• 英文别名: O-acetyl homoserine；(2S)-4-acetoxy-2-ammoniobutanoate；(2S)-4-acetyloxy-2-azaniumylbutanoate
• CAS: 7540-67-2
• 化学式: C₆H₁₁NO₄
• 分子量: 161.158
• InChiKey: FCXZBWSIAGGPCB-YFKPBYRVSA-N

物化性质

• 熔点：
  134-136°C
• 沸点：
  327.7±37.0 °C(Predicted)
• 密度：
  1.242±0.06 g/cm3(Predicted)
• 溶解度：
  甲醇（微溶）、水（微溶）
• 稳定性/保质期：
  如果按照规格使用和储存，则不会分解。

计算性质

• 辛醇/水分配系数(LogP)：
  -3.8
• 重原子数：
  11
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  89.6
• 氢给体数：
  2
• 氢受体数：
  5

安全信息

• 海关编码：
  2922509090
• 储存条件：
  密封于阴凉干燥环境中。

反应信息

• 作为反应物：
  描述：

  O-乙酰基-L-高丝氨酸 在 O-acetylhomoserine sulfhydrylase 、 硫化氢 作用下， 生成 L-高半胱氨酸
  参考文献：
  名称：

  O-乙酰高丝氨酸巯基化酶的鉴定，一种在艰难梭菌中负责蛋氨酸生物合成的假定酶：基因克隆和生化表征

  摘要：

  O-乙酰高丝氨酸巯基化酶 (OAHS) 是一种参与微生物蛋氨酸生物合成的吡哆醛 5'-磷酸依赖性酶。在这项研究中，我们报告了来自艰难梭菌的 OAHS 的基因克隆、蛋白质纯化和一些生化特征。该酶是分子量为 185 kDa 的四聚体。它在 L-同型半胱氨酸合成反应中具有高活性，可与其他来源的 OAHS 的报道活性相媲美。OAHS 活性受到代谢终产物 L-甲硫氨酸的抑制。L-Propargylglycine 被发现是该酶的自杀抑制剂。底物类似物 Nγ-乙酰基-L-2,4-二氨基丁酸是 OAHS 的竞争性抑制剂，Ki = 0.04 mM。艰难梭菌基因组分析表明该细菌使用直接巯基化的方式合成 L-甲硫氨酸。

  DOI：

  10.1002/iub.2139
• 作为产物：
  描述：

  L-高丝氨酸 在 乙酸酐 作用下， 生成 O-乙酰基-L-高丝氨酸
  参考文献：
  名称：

  IMPROVED PROCESS FOR SYNTHESIZING FUNCTIONALIZED MERCAPTANS

  摘要：

  The present invention relates to a process for synthesizing functionalized mercaptans essentially in the absence of oxygen, and also to a composition making it possible in particular to implement this process. Said functionalized mercaptans are of the following formula (I): in which, R 1 and R 7 , which are identical or different, are a hydrogen atom or an aromatic or nonaromatic, linear, branched or cyclic, saturated or unsaturated, hydrocarbon chain of 1 to 20 carbon atoms which may comprise one or more heteroatoms; X is chosen from -C(=O)-, -CH 2 - or -CN; R 2 is: (i) either absent when X represents -CN, (ii) or a hydrogen atom, (iii) or -OR 3 , R 3 being a hydrogen atom or an aromatic or nonaromatic, linear, branched or cyclic, saturated or unsaturated, hydrocarbon chain of 1 to 20 carbon atoms which may comprise one or more heteroatoms, (iv) or -NR 4 R 5 , R 4 and R 5 , which are identical or different, being a hydrogen atom or an aromatic or nonaromatic, linear, branched or cyclic, saturated or unsaturated, hydrocarbon chain of 1 to 20 carbon atoms which may comprise one or more heteroatoms; n is equal to 1 or 2; and * represents an asymmetric carbon.

  公开号：

  US20230295080A1

文献信息

• Biosynthesis of Mycotoxin Fusaric Acid and Application of a PLP-Dependent Enzyme for Chemoenzymatic Synthesis of Substituted <scp>l</scp>-Pipecolic Acids
  作者：Yang Hai、Mengbin Chen、Arthur Huang、Yi Tang

  DOI：10.1021/jacs.0c09352

  日期：2020.11.18

  synthesizing the picolinic acid scaffold. FA biosynthesis also involves an off-line collaboration between a highly reducing polyketide synthase (HRPKS, Fub1) and a nonribosomal peptide synthetase (NRPS)-like carboxylic acid reductase (Fub8) in making an aliphatic α,β-unsaturated aldehyde. By harnessing the stereoselective C-C bond-forming activity of Fub7, we established a chemoenzymatic route for stereoconvergent

  Fusaric acid (FA) 是一种众所周知的真菌毒素，在植物病理学中起重要作用。FA 的生物合成基因簇已被鉴定，但生物合成途径仍未阐明。在这里，我们阐明了 FA 的生物合成，其特征是在合成吡啶甲酸支架。FA 生物合成还涉及高度还原性聚酮化合物合酶 (HRPKS, Fub1) 和非核糖体肽合成酶 (NRPS) 样羧酸还原酶 (Fub8) 之间的离线协作，以制备脂肪族 α,β-不饱和醛。通过利用 Fub7 的立体选择性 CC 键形成活性，
• Method for Producing Bio-Based Homoserine Lactone and Bio-Based Organic Acid from O-Acyl Homoserine Produced by Microorganisms
  申请人：CJ Cheiljedang Corporation

  公开号：US20140296466A1

  公开（公告）日：2014-10-02

  The present invention relates to a method of producing bio-based homoserine lactone and bio-based organic acid through hydrolysis of O-acyl homoserine produced by a microorganism in the presence of an acid catalyst. According to the present invention, O-acyl homoserine produced by a microorganism is used as a raw material for producing 1,4-butanediol, gamma-butyrolactone, tetrahydrofuran and the like, which are industrially highly useful. The O-acyl homoserine produced by a microorganism can substitute conventional petrochemical products, can solve environmental concerns, including the emission of pollutants and the exhaustion of natural resources, and can be continuously renewable so as not to exhaust natural resources.

  本发明涉及一种通过在酸催化剂存在下水解微生物产生的O-酰基同型半胱氨酸，生产基于生物的同型半胱氨酸内酯和基于生物的有机酸的方法。根据本发明，利用微生物产生的O-酰基同型半胱氨酸作为原料，生产1,4-丁二醇、γ-丁内酯、四氢呋喃等工业上非常有用的产品。微生物产生的O-酰基同型半胱氨酸可以替代传统的石化产品，可以解决环境问题，包括污染物排放和自然资源枯竭，并且可以持续可再生，不会耗尽自然资源。
• Coupling Bioorthogonal Chemistries with Artificial Metabolism: Intracellular Biosynthesis of Azidohomoalanine and Its Incorporation into Recombinant Proteins
  作者：Ying Ma、Hernán Biava、Roberto Contestabile、Nediljko Budisa、Martino di Salvo

  DOI：10.3390/molecules19011004

  日期：——

  methodology based on genetic engineering of metabolic pathways for direct intracellular production of non-canonical amino acids from simple precursors, coupled with expanded genetic code. In particular, we engineered the intracellular biosynthesis of L-azidohomoalanine from O-acetyl-L-homoserine and NaN3, and achieved its direct incorporation into recombinant target proteins by AUG codon reassignment in

  在本文中，我们提出了一种基于代谢途径基因工程的新型“单一实验”方法，用于从简单前体直接在细胞内生产非规范氨基酸，并结合扩展的遗传密码。特别是，我们设计了从 O-乙酰基-L-高丝氨酸和 NaN3 细胞内生物合成 L-叠氮基高丙氨酸，并通过 AUG 密码子重新分配在甲硫氨酸-营养缺陷型大肠杆菌菌株中将其直接掺入重组靶蛋白中。在我们的系统中，宿主的蛋氨酸生物合成途径首先通过利用来自谷氨酸棒杆菌的重组磷酸吡哆醛依赖性 O-乙酰高丝氨酸巯基化酶的广泛反应特异性转向生产所需的非规范氨基酸。然后，完成了目标蛋白 barstar 的表达，并伴随着有效的 L-叠氮高丙氨酸掺入代替 L-甲硫氨酸。这项工作是原理验证，并为直接从常见的可发酵来源进行生物技术相关的非规范氨基酸的细胞内生产和位点特异性掺入的额外工作铺平了道路。
• Reactions of <i>O</i>-Substituted <scp>L</scp>-Homoserines Catalyzed by <scp>L</scp>-Methionine γ-Lyase and Their Mechanism
  作者：Nobuyoshi Esaki、Torn Nakayama、Seiji Sawada、Hidehiko Tanaka、Kenji Soda

  DOI：10.1080/00021369.1984.10866438

  日期：1984.8.1

  L-Methionine γ-lyase (EC 4.4.1.11) catalyzes α,γ-elimination of O-substituted L-homoserines (i.e., ROCH2CH2CH(NH2)COOH; R = acetyl, succinyl, or ethyl) to produce α-ketobutyrate, ammonia, and the corresponding carboxylate or alcohol, and also their γ-replacement reactions with various thiols to produce the corresponding S-substituted L-homocysteines. The reactivities of O-substituted L-homoserines in α,γ-elimination relative to that of L-methionine were as follows: O-acetyl, 140%; O-succinyl, 17%; and O-ethyl-L-homoserine, 99%. However, the enzyme does not catalyze the synthesis of O-substituted L-homoserines from alcohol or carboxylic acids in a γ-replacement reaction. We have analyzed the α,γ-elimination of O-acetyl-L-homoserine in deuterium oxide by 1H-NMR. The [β-2H, γ-2H]-species of α-ketobutyrate was exclusively formed from O-acetyl-L-homoserine. The enzyme catalyzes deamination of L-vinylglycine to give the identically labeled α-ketobutyrate species. Incubation of the enzyme with O-acetyl-L-homoserine resulted in the appearance of a new absorption band at 480 nm, which was observed also with L-vinylglycine. These results strongly suggest that the α,γ-elimination and γ-replacement reactions of O-acetyl-L-homoserine proceed through the stabilized α-carbanion of a Schiff base between pyridoxal 5'-phosphate and vinylglycine, which has been suggested as the key intermediate of L-methionine γ-lyase-caralyzed reactions of S-substituted L-homocysteines [N. Esaki, T. Suzuki, H. Tanaka, K. Soda and R. R. Rando, FEBS Lett., 84, 309 (1977).

  L-Methionine γ-裂解酶（EC 4.4.1.11）催化 O-取代的 L-高丝氨酸（即：ROCH2CH2CH(NH2)COOH；R = 乙酰基或乙基）的 α,γ-消除、ROCH2CH2CH(NH2)COOH；R = 乙酰基、琥珀酰基或乙基），生成 α-酮丁酸酯、氨和相应的羧酸酯或醇，以及它们与各种硫醇的 γ-置换反应，生成相应的 S-取代的 L-高半胱氨酸。与 L-蛋氨酸相比，O-取代的 L-高丝氨酸在 α,γ-消除反应中的反应活性如下：O-乙酰基为 140%；O-琥珀酰为 17%；O-乙基-L-高丝氨酸为 99%。然而，该酶不能催化以醇或羧酸为原料的 O-取代型 L-高丝氨酸的γ-置换反应。我们通过 1H-NMR 分析了 O-乙酰基-L-高丝氨酸在氧化氘中的α,γ-消除反应。α-酮丁酸的[β-2H, γ-2H]种类完全由 O-乙酰基-L-高丝氨酸形成。该酶催化 L-乙烯基甘氨酸的脱氨反应，从而产生标记相同的 α-酮丁酸。将该酶与 O-乙酰基-L-高丝氨酸混合后，在 480 纳米波长处出现了一条新的吸收带，在与 L-乙烯基甘氨酸混合时也观察到了这一现象。这些结果有力地表明，O-乙酰基-L-高丝氨酸的 α、γ-消除和 γ-置换反应是通过 5'- 磷酸吡哆醛和乙烯基甘氨酸之间的希夫碱的稳定化 α-碳酰基进行的。Esaki、T. Suzuki、H. Tanaka、K. Soda 和 R. R. Rando，FEBS Lett.，84，309（1977 年）。
• Use of dimethyl disulfide for methionine production in microoragnisms
  申请人：Zelder Oskar

  公开号：US20090281353A1

  公开（公告）日：2009-11-12

  The present invention features improved processes and organisms for the production of methionine. The invention demonstrates that a ΔmetF organism or a ΔmetE AmetH organism, for example, mutants of C. glutamicum or E. coli , can use a methyl capped sulfide source, e.g., dimethyl disulfide (DMDS), as a source of both sulfur and a methyl group, bypassing the need for MetH/MetE and MetF activity and the need to reduce sulfate, for the synthesis of methionine. Also described in this patent are data implicating MetY (also called MetZ) as an enzyme that incorporates a methyl capped sulfide source, e.g., DMDS, into methionine. A ΔmetF ΔmetB strain of C. glutamicum can use a methyl capped sulfide source, e.g., DMDS, as a source of both sulfide and a methyl group. Furthermore, methionine production by engineered prototrophic organisms that overproduce O-acetyl-homoserine was improved by the addition of a methyl capped sulfide source, e.g., DMDS.

  本发明涉及改进的方法和生物体，用于甲硫氨酸的生产。该发明表明，例如C. glutamicum或E. coli的ΔmetF生物体或ΔmetE AmetH生物体，可以使用甲基硫醚源，例如二甲基二硫化物（DMDS），作为硫和甲基的来源，绕过对甲硫氨酸合成所需的MetH/MetE和MetF活性以及还原硫酸的需要。本专利还描述了数据，暗示MetY（也称为MetZ）是一种将甲基硫醚源，例如DMDS，嵌入到甲硫氨酸中的酶。C. glutamicum的ΔmetF ΔmetB菌株可以使用甲基硫醚源，例如DMDS，作为硫和甲基的来源。此外，通过添加甲基硫醚源，例如DMDS，改进了通过过度产生O-乙酰同型半胱氨酸的工程原核生物的甲硫氨酸产量。