oxaloacetaldehyde | 20602-39-5

• 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: oxaloacetaldehyde
• 英文别名: 3,4-Dioxobutanoic acid
• CAS: 20602-39-5
• 化学式: C₄H₄O₄
• 分子量: 116.073
• InChiKey: BBCMXQMKOHQERY-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.7
• 重原子数：
  8
• 可旋转键数：
  3
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.25
• 拓扑面积：
  71.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  3-(3-吲哚基)-2-氧代丙酸 、 oxaloacetaldehyde 在 氢氧化钾 、 盐酸 作用下， 以 水 为溶剂， 反应 24.0h， 以53.3%的产率得到4-hydroxy-4-(3-indolylmethyl)-2-ketoglutaric acid
  参考文献：
  名称：

  Process of producing glutamate derivatives

  摘要：

  本发明涉及一种通过在催化同种转化的酶存在下，将式（1）的取代α-酮酸转化为式（2）的谷氨酸衍生物（包括其盐）如莫那汀的高效生产方法。

  公开号：

  US07297800B2

文献信息

• Discovery of McbB, an Enzyme Catalyzing the β-Carboline Skeleton Construction in the Marinacarboline Biosynthetic Pathway
  作者：Qi Chen、Changtao Ji、Yongxiang Song、Hongbo Huang、Junying Ma、Xinpeng Tian、Jianhua Ju

  DOI：10.1002/anie.201303449

  日期：2013.9.16

  Three genes, mcbABC, that drive the biosynthesis of marinacarbolines, have been elucidated through genome mining, gene inactivation, heterologous expression, feeding, and site‐directed mutagenesis experiments. McbB is highlighted as a novel enzyme for the β‐carboline core construction, which involves a Pictet–Spengler cyclization process and requiring E97 for biochemical activity.

  三个基因，mcbABC，推动marinacarbolines的生物合成，已通过基因组挖掘，基因失活，异源表达，饲养和定点突变实验阐明。McbB被强调为一种β-咔啉核心结构的新型酶，它涉及Pictet-Spengler环化过程，并且需要E 97才能具有生化活性。
• Structural Basis for β-Carboline Alkaloid Production by the Microbial Homodimeric Enzyme McbB
  作者：Takahiro Mori、Shotaro Hoshino、Shusaku Sahashi、Toshiyuki Wakimoto、Takashi Matsui、Hiroyuki Morita、Ikuro Abe

  DOI：10.1016/j.chembiol.2015.06.006

  日期：2015.7

  The beta-carboline (beta C) alkaloids occur throughout nature and exhibit diverse biological activities. In contrast to beta C alkaloid synthesis in plants, the biosynthesis in microorganisms remains poorly understood. The recently reported McbB from Marinactinospora thermotolerans is a novel enzyme proposed to catalyze the Pictet-Spengler (PS) reaction of L-tryptophan and oxaloacetaldehyde to produce the beta C scaffold of marinacarbolines. In this study, we solved the crystal structure of McbB complexed with L-tryptophan at 2.48 angstrom resolution, which revealed the novel protein folding of McbB and the totally different structure from those of other PS condensation catalyzing enzymes, such as strictosidine synthase and norcoclaurine synthase from plants. Structural analysis and site-directed mutagenesis confirmed that the previously proposed catalytic Glu97 at the active-site center functions as an acid and base catalyst. Remarkably, the structure-based mutants R72A and H87A, with expanded active-site cavities, newly accepted bulky phenylglyoxal as the aldehyde substrate, to produce 1-benzoyl-3-carboxy-beta-carboline.