L-N-gamma-Aminoarginine | 57444-72-1

• 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-N-gamma-Aminoarginine
• 英文别名: Nω-amino-L-arginine；Nω-amino-L-Arg-OH；NG-amino-L-arginine；Nw-amino-L-arginine；N^G-amino-L-arginine；omega-Aminoarginine；(2S)-2-amino-5-[[amino(hydrazinyl)methylidene]amino]pentanoic acid
• CAS: 57444-72-1
• 化学式: C₆H₁₅N₅O₂
• 分子量: 189.217
• InChiKey: NCHSYZVVWKVWFQ-BYPYZUCNSA-N

物化性质

• 沸点：
  384.4±52.0 °C(Predicted)
• 密度：
  1.53±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -4.5
• 重原子数：
  13
• 可旋转键数：
  6
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  140
• 氢给体数：
  5
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-N-gamma-Aminoarginine 在 alpha-酮戊二酸 、 recombinant Giardia lamblia arginine deiminase 、 水 、 还原型辅酶Ⅰ 作用下， 生成 L-瓜氨酸
  参考文献：
  名称：

  Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia

  摘要：

  Giardia lamblia arginine deiminase (GlAD), the topic of this paper, belongs to the hydrolase branch of the guanidine-modifying enzyme superfamily, whose members employ Cys-mediated nucleophilic catalysis to promote deimination of L-arginine and its naturally occurring derivatives. G. lamblia is the causative agent in the human disease giardiasis. The results of RNAi/antisense RNA gene-silencing studies reported herein indicate that GlAD is essential for G. lamblia trophozoite survival and thus, a potential target for the development of therapeutic agents for the treatment of giardiasis. The homodimeric recombinant protein was prepared in Escherichia coli for in-depth biochemical characterization. The 2-domain GlAD monomer consists of a N-terminal domain that shares an active site structure (depicted by an in silico model) and kinetic properties (determined by steady-state and transient state kinetic analysis) with its bacterial AD counterparts, and a C-terminal domain of unknown fold and function. GlAD was found to be active over a wide pH range and to accept L-arginine, L-arginine ethyl ester, N-alpha-benzoyl-L-arginine, and N-omega-amino-L-arginine as substrates but not agmatine, L-homoarginine, N-alpha-benzoyl- L-arginine ethyl ester or a variety of arginine-containing peptides. The intermediacy of a Cys424-alkylthiouronium ion covalent enzyme adduct was demonstrated and the rate constants for formation (k(1) = 80 s(-1)) and hydrolysis (k(2) = 35 s(-1)) of the intermediate were determined. The comparatively lower value of the steady-state rate constant (k(cat) = 2.6 s(-1)), suggests that a step following citrulline formation is rate-limiting. Inhibition of GlAD using Cys directed agents was briefly explored. S-Nitroso-L-homocysteine was shown to be an active site directed, irreversible inhibitor whereas N omega-cyano-L-arginine did not inhibit GlAD but instead proved to be an active site directed, irreversible inhibitor of the Bacillus cereus AD. (C) 2009 Published by Elsevier Inc.

  DOI：

  10.1016/j.bioorg.2009.06.001
• 作为产物：
  描述：

  、 N'-硝基-L-精氨酸 在 氧化铂 氢气 、 氩 、 水 、 黄胺酸 、 sodium hydroxide 、 盐酸 、 乙醇 、 乙醚 、 OH 、 四磷十氧化物 作用下， 以 溶剂黄146 为溶剂， 反应 113.17h， 生成 L-N-gamma-Aminoarginine
  参考文献：
  名称：

  Method of using aminoarginine to block nitric oxide formation in vitro

  摘要：

  纯度合适的生理活性N.sup.G-氨基精氨酸（即L或D，L形式）或其药学上可接受的盐以一定的抑制一氧化氮合成的剂量被给予需要这种抑制的受试者（例如低血压或需要免疫抑制效果的受试者），或者被添加到含有分离器官、完整细胞、细胞匀浆或组织匀浆的培养基中，以足够的剂量抑制一氧化氮的形成，以阐明或控制一氧化氮的生物合成、代谢或生理作用。N.sup.G-氨基-L-精氨酸通过还原N.sup.G-硝基-L-精氨酸，将L-精氨酸副产物转化为L-鸟氨酸并将N.sup.G-氨基-L-精氨酸与L-鸟氨酸分离而制备和分离为药学纯化合物。N.sup.G-氨基-D，L-精氨酸是通过类似的方法从N.sup.G-硝基-D，L-精氨酸开始制备的。

  公开号：

  US05158883A1

文献信息

• Isolating aminoarginine and use to block nitric oxide formation in body
  申请人：Cornell Research Foundation, Inc.

  公开号：US05059712A1

  公开（公告）日：1991-10-22

  Pharmaceutically pure physiologically active N.sup.G -aminoarginine (i.e., the L or D,L form) or pharmaceutically acceptable salt thereof is administered in a nitric oxide synthesis inhibiting amount to a subject in need of such inhibition (e.g. a subject with low blood pressure or needing immunosuppressive effect) or is added to a medium containing isolated organs, intact cells, cell homogenates or tissue homogenates in an amount sufficient to inhibit nitric oxide formation to elucide or control the biosynthesis, metabolism or physiological role of nitric oxide. N.sup.G -amino-L-arginine is prepared and isolated as a pharmaceutically pure compound by reducing N.sup.G -nitro-L-arginine, converting L-arginine by-product to L-ornithine with arginase and separating N.sup.G -amino-L-arginine from the L-ornithine. N.sup.G -amino-D,L-arginine is prepared in similar fashion starting with N.sup.G -nitro-D,L-arginine.

  纯度高的生理活性N.sup.G-氨基精氨酸（即L或D，L形式）或其药学上可接受的盐以抑制一定量的一氧化氮合成被施用给需要这种抑制的受试者（例如，低血压或需要免疫抑制作用的受试者），或者在含有分离的器官、完整的细胞、细胞匀浆或组织匀浆的培养基中添加足够的量以抑制一氧化氮的形成，以阐明或控制一氧化氮的生物合成、代谢或生理作用。通过还原N.sup.G-硝基-L-精氨酸，将L-精氨酸副产物转化为L-鸟氨酸，并从L-鸟氨酸中分离出N.sup.G-氨基-L-精氨酸，制备和分离纯度高的N.sup.G-氨基-L-精氨酸。类似地，从N.sup.G-硝基-D，L-精氨酸开始，以相似的方式制备N.sup.G-氨基-D，L-精氨酸。
• Inhibitors of nitric oxide biosynthesis
  申请人：Merrell Dow Pharmaceuticals Inc.

  公开号：US05318992A1

  公开（公告）日：1994-06-07

  The present invention is a method of treating hypotension and shock using select ornithine or N.sup.G -arginine derivatives.

  本发明是一种使用特定的鸟氨酸或N.sup.G-精氨酸衍生物治疗低血压和休克的方法。
• US9574190B2
  申请人：——

  公开号：US9574190B2

  公开（公告）日：2017-02-21
• Mechanisms of catalysis and inhibition operative in the arginine deiminase from the human pathogen Giardia lamblia
  作者：Zhimin Li、Liudmila Kulakova、Ling Li、Andrey Galkin、Zhiming Zhao、Theodore E. Nash、Patrick S. Mariano、Osnat Herzberg、Debra Dunaway-Mariano

  DOI：10.1016/j.bioorg.2009.06.001

  日期：2009.10

  Giardia lamblia arginine deiminase (GlAD), the topic of this paper, belongs to the hydrolase branch of the guanidine-modifying enzyme superfamily, whose members employ Cys-mediated nucleophilic catalysis to promote deimination of L-arginine and its naturally occurring derivatives. G. lamblia is the causative agent in the human disease giardiasis. The results of RNAi/antisense RNA gene-silencing studies reported herein indicate that GlAD is essential for G. lamblia trophozoite survival and thus, a potential target for the development of therapeutic agents for the treatment of giardiasis. The homodimeric recombinant protein was prepared in Escherichia coli for in-depth biochemical characterization. The 2-domain GlAD monomer consists of a N-terminal domain that shares an active site structure (depicted by an in silico model) and kinetic properties (determined by steady-state and transient state kinetic analysis) with its bacterial AD counterparts, and a C-terminal domain of unknown fold and function. GlAD was found to be active over a wide pH range and to accept L-arginine, L-arginine ethyl ester, N-alpha-benzoyl-L-arginine, and N-omega-amino-L-arginine as substrates but not agmatine, L-homoarginine, N-alpha-benzoyl- L-arginine ethyl ester or a variety of arginine-containing peptides. The intermediacy of a Cys424-alkylthiouronium ion covalent enzyme adduct was demonstrated and the rate constants for formation (k(1) = 80 s(-1)) and hydrolysis (k(2) = 35 s(-1)) of the intermediate were determined. The comparatively lower value of the steady-state rate constant (k(cat) = 2.6 s(-1)), suggests that a step following citrulline formation is rate-limiting. Inhibition of GlAD using Cys directed agents was briefly explored. S-Nitroso-L-homocysteine was shown to be an active site directed, irreversible inhibitor whereas N omega-cyano-L-arginine did not inhibit GlAD but instead proved to be an active site directed, irreversible inhibitor of the Bacillus cereus AD. (C) 2009 Published by Elsevier Inc.
• Method of using aminoarginine to block nitric oxide formation in vitro
  申请人：Cornell Research Foundation, Inc.

  公开号：US05158883A1

  公开（公告）日：1992-10-27

  Pharmaceutically pure physiologically active N.sup.G -aminoarginine (i.e., the L or D,L form) or pharmaceutically acceptable salt thereof is administered in a nitric oxide synthesis inhibiting amount to a subject in need of such inhibition (e.g. a subject with low blood pressure or needing immunosuppressive effect) or is added to a medium containing isolated organs, intact cells, cell homogenates or tissue homogenates in an amount sufficient to inhibit nitric oxide formation to elucide or control the biosynthesis, metabolism or physiological role of nitric oxide. N.sup.G -amino-L-arginine is prepared and isolated as a pharmaceutically pure compound by reducing N.sup.G -nitro-L-arginine, converting L-arginine by-product to L-ornithine with arginase and separating N.sup.G -amino-L-arginine from the L-ornithine. N.sup.G -amino-D,L-arginine is prepared in similar fashion starting with N.sup.G -nitro-D,L-arginine.

  纯度合适的生理活性N.sup.G-氨基精氨酸（即L或D，L形式）或其药学上可接受的盐以一定的抑制一氧化氮合成的剂量被给予需要这种抑制的受试者（例如低血压或需要免疫抑制效果的受试者），或者被添加到含有分离器官、完整细胞、细胞匀浆或组织匀浆的培养基中，以足够的剂量抑制一氧化氮的形成，以阐明或控制一氧化氮的生物合成、代谢或生理作用。N.sup.G-氨基-L-精氨酸通过还原N.sup.G-硝基-L-精氨酸，将L-精氨酸副产物转化为L-鸟氨酸并将N.sup.G-氨基-L-精氨酸与L-鸟氨酸分离而制备和分离为药学纯化合物。N.sup.G-氨基-D，L-精氨酸是通过类似的方法从N.sup.G-硝基-D，L-精氨酸开始制备的。