L-3-oxoalanine | 205876-48-8

• 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: L-3-oxoalanine
• 英文别名: 2-amino-3-oxopropanoic acid；2-Aminomalonate semialdehyde；(2S)-2-azaniumyl-3-oxopropanoate
• CAS: 205876-48-8
• 化学式: C₃H₅NO₃
• 分子量: 103.078
• InChiKey: XMTCKNXTTXDPJX-REOHCLBHSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -3.7
• 重原子数：
  7
• 可旋转键数：
  2
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.33
• 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：

  L-3-oxoalanine 、 氢(+1)阳离子 生成 Ammonioacetaldehyde 、 二氧化碳
  参考文献：
  名称：

  Cloning and Sequencing of the Serine Dehydrogenase Gene fromAgrobacterium tumefaciens

  摘要：

  将来自农杆菌ICR 1600的NADP+依赖性丝氨酸脱氢酶[EC 1.1.1.-]的结构基因克隆到大肠杆菌细胞中，并对其完整的DNA序列进行了分析。该基因编码的多肽含有249个氨基酸残基。该酶与细菌的短链醇脱氢酶以及流感嗜血杆菌、大肠杆菌和酿酒酵母的未知蛋白具有高度的序列相似性。

  DOI：

  10.1271/bbb.66.1137
• 作为产物：
  描述：

  DL-丝氨酸 在 NADH oxidase 、 alcohol dehydrogenase isoenzyme E from Equus caballus 、 nicotinamide adenine dinucleotide phosphate 作用下， 以 aq. buffer 为溶剂， 生成 L-3-oxoalanine 、 (2R)-2-amino-3-oxopropanoic acid
  参考文献：
  名称：

  重新审视氨基醛

  摘要：

  研究氨基醇的酶促氧化以解决长期存在的产品稳定性问题。氨基醛是备受追捧的不稳定化合物，当它们立即受到保护时，可以在温和条件下生成。利用一系列醇脱氢酶 (ADH) 和氨基脲作为清除剂，可以对受保护的氨基醛进行对映选择性合成。来自氧化葡糖杆菌 (GoGDH) 的甘油脱氢酶显示出优异的对映选择性，但底物范围有限，而马肝 ADH 催化广泛的转化，但对映选择性较低。

  DOI：

  10.1002/ejoc.201701213

文献信息

• Nonenzymatic, Self-Elimination Degradation Mechanism of Glutathione
  作者：Manjeet Deshmukh、Hilliard Kutscher、Stanley Stein、Patrick Sinko

  DOI：10.1002/cbdv.200800277

  日期：2009.4

  In the present in vitro studies, evidence is provided showing that glutathione (GSH) can undergo spontaneous, nonenzymatic auto-degradation. The initial cleavage of the Glu-Cys bond involves nucleophilic attack of the N-terminal amino group of GSH at the gamma-carbonyl side chain, followed by an unusual cleavage of the Cys-Gly amide bond that is complete within 3-5 weeks in the physiological pH range

  在目前的体外研究中，提供的证据表明谷胱甘肽 (GSH) 可以发生自发的、非酶促的自降解。 Glu-Cys 键的初始裂解涉及 GSH N 端氨基在 γ-羰基侧链的亲核攻击，随后是 Cys-Gly 酰胺键的异常裂解，该裂解在 3-5 周内完成。生理pH范围。这些观察结果可能有助于开发新型可生物降解聚合物和可释放的前药，用于持续和靶向药物输送应用。
• Automated identification of peptides
  申请人：——

  公开号：US20020102610A1

  公开（公告）日：2002-08-01

  A fully automated, user-independent method is described for computer-mediated interpretation of data derived by mass spectrometry of an experimental peptide to identify and characterize a corresponding peptide sequence in a peptide database. The method identifies the corresponding sequence if it is present in the database, without the need for a skilled observer to choose from amongst a list of possible matches. By using an automated back-read process, the present method can uniquely identify a corresponding peptide sequence in a database based on a single matching peptide sequence. The method also permits mapping of mass spectral data to sequences in peptide or nucleotide databases for unambiguous identification of exons; determining a correct reading frame; identifying artefacts and errors in sequences; identifying mutations and polymorphisms; identifying post-translational modifications; and identifying exon-intron boundaries.

  本文描述了一种完全自动化、不依赖用户的方法，用于通过质谱技术获得的实验性肽段数据的计算机介导解释，以识别和表征相应的肽段序列在肽段数据库中的对应关系。该方法可以在不需要熟练的观察者从可能匹配的列表中选择的情况下，识别出数据库中存在的相应序列。通过使用自动化的反向读取过程，本方法可以基于单个匹配的肽段序列，在数据库中唯一地识别相应的肽段序列。该方法还允许将质谱数据映射到肽或核苷酸数据库中的序列，以明确识别外显子；确定正确的阅读框架；识别序列中的工件和错误；识别突变和多态性；识别后翻译修饰；以及识别外显子-内含子边界。
• A Novel NADP⁺-dependent Serine Dehydrogenase from<i>Agrobacterium tumefaciens</i>
  作者：Emran Kabir Chowdhury、Kazuhiko Higuchi、Shinji Nagata、Haruo Misono

  DOI：10.1271/bbb.61.152

  日期：1997.1

  NADP+-dependent serine dehydrogenase [EC 1.1.1.–], which catalyzes the oxidation of the hydroxyl group of serine to form 2-aminomalonate semialdehyde, was purified to homogeneity from a crude extract of Agrobacterium tumefaciens ICR 1600. The enzyme had a molecular mass of about 100 kDa and consisted of four identical subunits. In addition to l-serine, d-serine, l-glycerate, d-glycerate, and 2-methyl-dl-serine were substrates. However, O-methyl-dl-serine and l-threonine were inert. The enzyme showed maximal activity at about pH 9 for the oxidation of l-serine. The enzyme required NADP+ as a coenzyme, NAD + was inert. The enzyme was not inhibited by EDTA, o-phenanthroline, or α, α′-dipyridyl, but was inhibited by HgCl2, p-chloromercuribenzoate, l-cysteine, d-cysteine, malonate, 2-methylmalonate, and tartronate. The Michaelis constants for l-serine, d-serine, and NADP+ were 42, 44, and 0.029 mm, respectively.

  依赖NADP+的丝氨酸脱氢酶（EC 1.1.1.）催化丝氨酸羟基的氧化反应，生成2-氨基丙二酸半醛。该酶从农杆菌ICR 1600的粗提物中纯化得到，纯度很高。该酶的分子质量约为100 kDa，由四个相同的亚基组成。除了l-丝氨酸、d-丝氨酸、l-甘油酸、d-甘油酸和2-甲基-dl-丝氨酸是底物外，O-甲基-dl-丝氨酸和l-苏氨酸是惰性的。该酶在pH 9左右对l-丝氨酸的氧化反应表现出最大的活性。该酶需要NADP+作为辅酶，NAD+是惰性的。EDTA、邻菲罗啉或α,α′-二吡啶不能抑制该酶，但HgCl2、对氯汞苯甲酸盐、l-半胱氨酸、d-半胱氨酸、丙二酸盐、2-甲基丙二酸盐和酒石酸盐可以抑制该酶。l-丝氨酸、d-丝氨酸和NADP+的Michaelis常数分别为42、44和0.029 mm。
• Characterization of short-chain dehydrogenase/reductase homologues of Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C)
  作者：Hisae Fujisawa、Shinji Nagata、Haruo Misono

  DOI：10.1016/s1570-9639(02)00533-2

  日期：2003.1

  Short-chain dehydrogenase/reductase homologues from Escherichia coli (YdfG) and Saccharomyces cerevisiae (YMR226C) show high sequence similarity to serine dehydrogenase from Agrobacterium tumefaciens. We cloned each gene encoding YdfG and YMR226C into E. coli JM109 and purified them to homogeneity from the E. coli clones. YdfG and YMR226C consist of four identical subunits with a molecular mass of 27 and 29 kDa, respectively. Both enzymes require NADP(+) as a coenzyme and use L-serine as a substrate. Both enzymes show maximum activity at about pH 8.5 for the oxidation of L-serine. They also catalyze the oxidation of D-serine, L-allo-threonine, D-threonine, 3-hydroxyisobutyrate, and 3-hydroxybutyrate. The k(cat)/K-m values of YdfG for L-serine, D-serine, L-allo-threonine, D-threonine, L-3-hydroxyisobutyrate, and D-3-hydroxyisobutyrate are 105, 29, 199, 109, 67, and 62 M-1 s(-1), and those of YMR226C are 116, 110, 14600, 7540, 558, and 151 M-1 s(-1), respectively. Thus, YdfG and YMR226C are NADP(+)-dependent dehydrogenases acting on 3-hydroxy acids with a three- or four-carbon chain, and L-allo-threonine is the best substrate for both enzymes. (C) 2002 Elsevier Science B.V. All rights reserved.
• Biochemical and Structural Studies of Uncharacterized Protein PA0743 from Pseudomonas aeruginosa Revealed NAD+-dependent l-Serine Dehydrogenase
  作者：Anatoli Tchigvintsev、Alexander Singer、Greg Brown、Robert Flick、Elena Evdokimova、Kemin Tan、Claudio F. Gonzalez、Alexei Savchenko、Alexander F. Yakunin

  DOI：10.1074/jbc.m111.294561

  日期：2012.1

  The β-hydroxyacid dehydrogenases form a large family of ubiquitous enzymes that catalyze oxidation of various β-hydroxy acid substrates to corresponding semialdehydes. Several known enzymes include β-hydroxyisobutyrate dehydrogenase, 6-phosphogluconate dehydrogenase, 2-(hydroxymethyl)glutarate dehydrogenase, and phenylserine dehydrogenase, but the vast majority of β-hydroxyacid dehydrogenases remain uncharacterized. Here, we demonstrate that the predicted β-hydroxyisobutyrate dehydrogenase PA0743 from Pseudomonas aeruginosa catalyzes an NAD(+)-dependent oxidation of l-serine and methyl-l-serine but exhibits low activity against β-hydroxyisobutyrate. Two crystal structures of PA0743 were solved at 2.2-2.3-Å resolution and revealed an N-terminal Rossmann fold domain connected by a long α-helix to the C-terminal all-α domain. The PA0743 apostructure showed the presence of additional density modeled as HEPES bound in the interdomain cleft close to the predicted catalytic Lys-171, revealing the molecular details of the PA0743 substrate-binding site. The structure of the PA0743-NAD(+) complex demonstrated that the opposite side of the enzyme active site accommodates the cofactor, which is also bound near Lys-171. Site-directed mutagenesis of PA0743 emphasized the critical role of four amino acid residues in catalysis including the primary catalytic residue Lys-171. Our results provide further insight into the molecular mechanisms of substrate selectivity and activity of β-hydroxyacid dehydrogenases.