D-aspartate | 5976-97-6

• 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: D-aspartate
• 英文别名: (2R)-2-aminobutanedioate
• CAS: 5976-97-6
• 化学式: C₄H₅NO₄
• 分子量: 131.088
• InChiKey: CKLJMWTZIZZHCS-UWTATZPHSA-L

计算性质

• 辛醇/水分配系数(LogP)：
  -2.6
• 重原子数：
  9
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  106
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  D-aspartate 、 S-腺苷-L-蛋氨酸 在 D-aspartate N-methyltransferase from the pancreas of mouse 作用下， 以 aq. buffer 为溶剂， 反应 0.33h， 以100%的产率得到N-methyl-D-aspartate
  参考文献：
  名称：

  d-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-d-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice

  摘要：

  N-Methyl-D-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of D-aspartate N-methyltransferase (DDNMT), which produces NMDA from D-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for D-aspartate and is S-adenosyl-L-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).

  DOI：

  10.1016/j.bbapap.2020.140527

文献信息

• ASPARTATE OF 1-CYCLOPROPYL-6-FLUORO-7-(8-METHOXYIMINO-2,6-DIAZA-SPIRO[3.4]OCT-6-YL)-4-OXO-1,4-DIHYDRO-[1,8]NAPHTHYRIDINE-3-CARBOXYLIC ACID, METHOD FOR PREPARING THE SAME, AND ANTIMICROBIAL PHARMACEUTICAL COMPOSITION COMPRISING THE SAME
  申请人：Ryu Jei Man

  公开号：US20100184795A1

  公开（公告）日：2010-07-22

  Disclosed are aspartic acid salts of 1-cyclopropyl-6-fluoro-7-(8-methoxyimino-2,6-diaza-spiro[3.4]oct-6-yl)-4-oxo-1,4-dihydro-[1,8]naphthyridine-3-carboxylic acid, methods for preparing the same, and antimicrobial pharmaceutical compositions comprising the same.

  本发明涉及天冬氨酸盐的1-环丙基-6-氟-7-(8-甲氧基亚胺基-2,6-二氮杂螺[3.4]辛-6-基)-4-氧代-1,4-二氢-[1,8]萘啶-3-羧酸，其制备方法，以及包含它们的抗微生物制剂。
• Aspartate of 1-cyclopropyl-6-fluoro-7-(8-methoxyimino-2,6-diaza-spiro[3.4]oct-6-yl)-4-oxo-1,4-dihydro-[1,8]naphthyridine-3-carboxylic acid, method for preparing the same, and antimicrobial pharmaceutical composition comprising the same
  申请人：Dong Wha Pharmaceutical Co. Ltd.

  公开号：US08324238B2

  公开（公告）日：2012-12-04

  Disclosed are aspartic acid salts of 1-cyclopropyl-6-fluoro-7-(8-methoxyimino-2,6-diaza-spiro[3.4]oct-6-yl)-4-oxo-1,4-dihydro-[1,8]naphthyridine-3-carboxylic acid, methods for preparing the same, and antimicrobial pharmaceutical compositions comprising the same.

  本发明涉及1-环丙基-6-氟-7-(8-甲氧基亚胺基-2,6-二氮杂螺[3.4]辛-6-基)-4-氧代-1,4-二氢-[1,8]萘啉-3-羧酸的天冬氨酸盐，以及制备它们的方法和包含它们的抗微生物药物组合物。
• d-Aspartate N-methyltransferase catalyzes biosynthesis of N-methyl-d-aspartate (NMDA), a well-known selective agonist of the NMDA receptor, in mice
  作者：Kimihiko Shibata、Daiki Imanishi、Katsumasa Abe、Masataka Suzuki、Shouji Takahashi、Yoshio Kera

  DOI：10.1016/j.bbapap.2020.140527

  日期：2020.12

  N-Methyl-D-aspartate (NMDA), which is a selective agonist for the NMDA receptor, has recently been shown to be present in various biological tissues. In mammals, the activity of D-aspartate N-methyltransferase (DDNMT), which produces NMDA from D-aspartate, has been detected only in homogenates prepared from rat tissues. Moreover, the enzymatic properties of DDNMT have been poorly studied and its molecular entity has not yet been identified. In this report, we show for the first time that the activity of DDNMT is present in mouse tissues and succeed in obtaining a partially purified enzyme preparation from a mouse tissue homogenate with a purification fold of 1900 or more, and have characterized the enzymatic activity of this preparation. The results indicate that DDNMT, which is highly specific for D-aspartate and is S-adenosyl-L-methionine-dependent, is a novel enzyme that clearly differs from the known methylamine-glutamate N-methyltransferase (EC 2.1.1.21) and glycine N-methyltransferase (EC 2.1.1.20).