(S)-4-氨基-5-氧代戊酸 | 68462-55-5

• 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: (S)-4-氨基-5-氧代戊酸
• 英文名称: L-glutamic acid
• 英文别名: (S)-4-amino-5-oxopentanoate；(4S)-4-azaniumyl-5-oxopentanoate
• CAS: 68462-55-5
• 化学式: C₅H₉NO₃
• 分子量: 131.131
• InChiKey: MPUUQNGXJSEWTF-BYPYZUCNSA-N

物化性质

• 沸点：
  295.5±35.0 °C(Predicted)
• 密度：
  1.224±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.6
• 重原子数：
  9
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.6
• 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：

  (S)-4-氨基-5-氧代戊酸 在 双氧水 、 sodium bromide 作用下， 以 水 为溶剂， 反应 5.0h， 生成 3-氰基丙酸
  参考文献：
  名称：

  钒氯过氧化物酶对氨基酸进行选择性氧化脱羧以生产与工业相关的腈

  摘要：

  来自生物质的工业腈：钒-氯过氧化物酶已成功用于通过催化量的卤化物盐将谷氨酸选择性地转化为3-氰基丙酸，3-氰基丙酸是合成生物琥珀腈和生物丙烯腈的关键中间体。这种清洁的氧化脱羧作用可应用于从植物废物流中获得的氨基酸混合物，从而导致腈易于分离。

  DOI：

  10.1002/cssc.201200098
• 作为试剂：
  描述：

  palladium dichloride 在 硫酸 、 (S)-4-氨基-5-氧代戊酸 作用下， 以 水 为溶剂， 反应 0.25h， 生成 palladium
  参考文献：
  名称：

  Hierarchical wheat-like Au–Pd heterostructures with enhanced catalytic activity toward methanol electrooxidation

  摘要：

  In this report, a simple, facile, controllable, and green one-step electrochemical co-deposition method was developed for the preparation of hierarchical wheat-like Au-Pd heterostructures on a glassy carbon electrode (GCE) without any template or surfactant, only using L-glutamic acid as a growth directing agent. The control experiments associated with the applied potential, the molar ratio of HAuCl4 to PdCl2, electrodeposition time, and concentration of L-glutamic acid were investigated in details. Meanwhile, the electrochemical experiments demonstrate the superior electrocatalytic activity of the Au-Pd heterostructures toward methanol oxidation, achieving a maximum catalytic current density of 45.8 mA cm(-2) in the presence of 0.5 M methanol, much larger than those on pure Au (5.4 mA cm(-2)) or Pd (25.0 mA cm(-2)) under the same conditions. (C) 2013 Elsevier B.V. All rights reserved.

  DOI：

  10.1016/j.jallcom.2013.07.170

文献信息

• Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.
  作者：L L Ilag、A M Kumar、D Söll

  DOI：10.1105/tpc.6.2.265

  日期：1994.2

  5-Aminolevulinic acid (ALA) is the universal precursor of tetrapyrroles, such as chlorophyll and heme. The major control of chlorophyll biosynthesis is at the step of ALA formation. In the chloroplasts of plants, as in Escherichia coli, ALA is derived from the glutamate of Glu-tRNA via the two-step C5 pathway. The first enzyme, Glu-tRNA reductase, catalyzes the reduction of Glu-tRNA to glutamate 1-semialdehyde with the release of intact tRNA. The second enzyme, glutamate 1-semialdehyde 2,1-aminomutase, converts glutamate 1-semialdehyde to ALA. To further examine ALA formation in plants, we isolated Arabidopsis genes that encode the enzymes of the C5 pathway via functional complementation of mutations in the corresponding genes of E. coli. The Glu-tRNA reductase gene was designated HEMA and the glutamate 1-semialdehyde 2,1-aminomutase gene, GSA1. Each gene contains two short introns (149 and 241 nucleotides for HEMA, 153 and 86 nucleotides for GSA1). The deduced amino acid sequence of the HEMA protein predicts a protein of 60 kD with substantial similarity (30 to 47% identity) to sequences derived from the known hemA genes from microorganisms that make ALA by the C5 pathway. Purified Arabidopsis HEMA protein has Glu-tRNA reductase activity. The GSA1 gene encodes a 50-kD protein whose deduced amino acid sequence shows extensive homology (55 to 78% identity) with glutamate 1-semialdehyde 2,1-aminomutase proteins from other species. RNA gel blot analyses indicated that transcripts for both genes are found in root, leaf, stem, and flower tissues and that their levels are dramatically elevated by light. Thus, light may regulate ALA, and hence chlorophyll formation, by exerting coordinated transcriptional control over both enzymes of the C5 pathway.

  基因的转录。
• Glutamate-1-semialdehyde aminotransferase from <i>Sulfolobus solfataricus</i>
  作者：Gianna PALMIERI、Michela DI PALO、Andrea SCALONI、Stefania ORRÙ、Gennaro MARINO、Giovanni SANNIA

  DOI：10.1042/bj3200541

  日期：1996.12.1

  Glutamate-1-semialdehyde aminotransferase (GSA-AT) from the extremely thermophilic bacterium Sulfolobus solfataricus has been purified to homogeneity and characterized. GSA-AT is the last enzyme in the C5 pathway for the conversion of glutamate into the tetrapyrrole precursor Δ-aminolaevulinate (ALA) in plants, algae and several bacteria. The active form of GSA-AT from S. solfataricus seems to be a homodimer with a molecular mass of 87 kDa. The absorption spectrum of the purified aminotransferase is indicative of the presence of pyridoxamine 5´-phosphate (PMP) cofactor, and the catalytic activity of the enzyme is further stimulated by addition of PMP. 3-Amino-2,3-dihydrobenzoic acid is an inhibitor of the aminotransferase activity. The N-terminal amino acid sequence of GSA-AT from S. solfataricus was found to share significant similarity with the eukaryotic and eubacterial enzymes. Evidence is provided that ALA synthesis in S. solfataricus follows the C5 pathway characteristic of plants, algae, cyanobacteria and many other bacteria.

  从极端热嗜好菌Sulfolobus solfataricus中纯化并表征了谷氨酸-1-半醛氨基转移酶（GSA-AT）。GSA-AT是植物、藻类和几种细菌中将谷氨酸转化为四吡咯前体Δ-氨基戊酸（ALA）的C5途径中的最后一个酶。来自S. solfataricus的GSA-AT的活性形式似乎是一个分子量为87 kDa的同源二聚体。纯化的氨基转移酶的吸收光谱表明存在吡哆醇酮5'-磷酸（PMP）辅因子，并且酶的催化活性受到PMP的进一步刺激。 3-氨基-2,3-二氢苯甲酸是氨基转移酶活性的抑制剂。从S. solfataricus的GSA-AT的N末端氨基酸序列发现与真核生物和真细菌酶有显着相似性。提供了证据表明S. solfataricus中的ALA合成遵循植物、藻类、蓝细菌和许多其他细菌的C5途径。
• Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry
  作者：Steven Brody、Jens S. Andersen、C. Gamini Kannangara、Morten Meldgaard、Peter Roepstorff、Diter von Wettstein

  DOI：10.1021/bi00049a006

  日期：1995.12.12

  Synechococcus is pale yellow and has absorption maxima at 338 and 418 nm from vitamin B6. Yellow, colorless, and pink forms of the protein are obtained by treatment with 4,5-dioxovalerate, 4,5-diaminovalerate, and acetylenic GABA, respectively. Compared to the native enzyme, the 418 nm absorption maximum in the yellow enzyme is enhanced and the 338 nm maximum reduced while the colorless enzyme has a heightened

  谷氨酸1-半醛氨基转移酶产生δ-氨基乙酰丙酸酯，用于合成叶绿素，血红素和其他四吡咯颜料。来自Synechococcus的天然酶为浅黄色，在338和418 nm处吸收的维生素B6具有最大吸收。该蛋白质的黄色，无色和粉红色形式分别通过分别用4,5-二氧戊酸，4,5-二氨基戊酸和炔属GABA处理得到。与天然酶相比，黄色酶的最大418 nm吸收最大值增强，而338 nm的最大值减小，而无色酶在338 nm处具有最大最大值，在418 nm处几乎检测不到峰。粉红酶在560 nm处具有最大吸收。当天然和无色酶在0.5 M Na2HPO4，pH 7.0中重复稀释并重新浓缩时，吡ido胺5' 释放出磷酸盐，最大损失338 nm。因此，338 nm的最大吸收与非共价结合的吡amine胺5'-磷酸盐有关。NaBH4还原证明在418 nm处的吸光度是由Schiff碱基结合到蛋白质的吡ido醛5'-磷酸辅因子引起的
• Crystal structure of glutamate-1-semialdehyde aminomutase: An α ₂ -dimeric vitamin B ₆ -dependent enzyme with asymmetry in structure and active site reactivity
  作者：Michael Hennig、Bernhard Grimm、Roberto Contestabile、Robert A. John、Johan N. Jansonius

  DOI：10.1073/pnas.94.10.4866

  日期：1997.5.13

  The three-dimensional structure of glutamate-1-semialdehyde aminomutase (EC 5.4.3.8 ), an α ₂ -dimeric enzyme from Synechococcus, has been determined by x-ray crystallography using heavy atom derivative phasing. The structure, refined at 2.4-Å resolution to an R-factor of 18.7% and good stereochemistry, explains many of the enzyme’s unusual specificity and functional properties. The overall fold is that of aspartate aminotransferase and related B ₆ enzymes, but it also has specific features. The structure of the complex with gabaculine, a substrate analogue, shows unexpectedly that the substrate binding site involves residues from the N-terminal domain of the molecule, notably Arg-32. Glu-406 is suitably positioned to repel α-carboxylic acids, thereby suggesting a basis for the enzyme’s reaction specificity. The subunits show asymmetry in cofactor binding and in the mobilities of the residues 153–181. In the unliganded enzyme, one subunit has the cofactor bound as an aldimine of pyridoxal phosphate with Lys-273 and, in this subunit, residues 153–181 are disordered. In the other subunit in which the cofactor is not covalently bound, residues 153–181 are well defined. Consistent with the crystallographically demonstrated asymmetry, a form of the enzyme in which both subunits have pyridoxal phosphate bound to Lys-273 through a Schiff base showed biphasic reduction by borohydride in solution. Analysis of absorption spectra during reduction provided evidence of communication between the subunits. The crystal structure of the reduced form of the enzyme shows that, despite identical cofactor binding in each monomer, the structural asymmetry at residues 153–181 remains.

  谷氨酸-1-半胱氨酸氨基变位酶（EC 5.4.3.8），一种来自Synechococcus的α2-二聚酶的三维结构已通过重原子衍射确定。该结构在2.4埃分辨率下精细到18.7％的R因子和良好的立体化学，解释了该酶的许多不寻常的特异性和功能特性。总体折叠类似于天冬氨酸氨基转移酶和相关的B6酶，但也具有特定的特征。与底物类似物Gabaculine的复合物的结构意外地显示，底物结合位点涉及分子的N末端域的残基，特别是Arg-32。Glu-406适当地定位以排斥α-羧酸，因此建议了酶的反应特异性的基础。亚基在辅因子结合和残基153-181的运动性方面显示不对称性。在未配体化的酶中，一个亚基将辅因子作为吡哆醛磷酸的醛胺结合物与Lys-273结合，并且在该亚基中，残基153-181无序。在辅因子未共价结合的另一个亚基中，残基153-181定义明确。与晶体学证明的不对称性一致，酶的一种形式，其中两个亚基通过席夫碱将吡哆醛磷酸结合到Lys-273，溶液中显示双相还原。在还原过程中，吸收光谱的分析提供了亚基之间通信的证据。酶的还原形式的晶体结构显示，尽管每个单体的辅因子结合相同，但残基153-181的结构不对称性仍然存在。
• Escherichia coli Glutamyl-tRNA Reductase
  作者：Stefan Schauer、Shalini Chaturvedi、Lennart Randau、Jürgen Moser、Makoto Kitabatake、Stefan Lorenz、Elizabeth Verkamp、Wolf-Dieter Schubert、Toru Nakayashiki、Masatoshi Murai、Kristen Wall、Hans-Ulrich Thomann、Dirk W. Heinz、Hachiro Inokuchi、Dieter Söll、Dieter Jahn

  DOI：10.1074/jbc.m206924200

  日期：2002.12

  In the first step of tetrapyrrole biosynthesis in Escherichia coli, glutamyl-tRNA reductase (GluTR, encoded by hemA) catalyzes the NADPH-dependent reduction of glutamyl-tRNA to glutamate-l-semialdehyde. Soluble homodimeric E. coli GluTR was made by co-expressing the hemA gene and the chaperone genes dnaJK and grpE. During Mg2+-stimulated catalysis, the reactive sulfhydryl group of Cys-50 in the E. coli enzyme attacks the a-carbonyl group of the tRNA-bound glutamate. The resulting thioester intermediate was trapped and detected by autoradiography. In the presence of NADPH, the end product, glutamate-l-semialdehyde, is formed. In the absence of NADPH, E. coli GluTR exhibited substrate esterase activity. The in vitro synthesized unmodified glutamyl-tRNA was an acceptable substrate for E. coli GluTR. Eight 5-aminolevulinic acid auxotrophic E. coli hemA mutants were genetically selected, and the corresponding mutations were determined. Most of the recombinant purified mutant GluTR enzymes lacked detectable activity. Based on the Methanopyrus kandleri GluTR structure, the positions of the amino acid exchanges are close to the catalytic domain (G7D, E114K, R314C, S22L/S164F, G44C/S105N/A326T, G106N, S145F). Only GluTR G191D (affected in NADPH binding) revealed esterase but no reductase activity.