Iminoarginine

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 脂肪酰基
• 英文名称: Iminoarginine
• 英文别名: 5-(diaminomethylideneamino)-2-iminopentanoic acid
• 化学式: C₆H₁₂N₄O₂
• 分子量: 172.187
• InChiKey: YWGYOCPWFDUKSA-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -1.5
• 重原子数：
  12
• 可旋转键数：
  5
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.5
• 拓扑面积：
  126
• 氢给体数：
  4
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  Iminoarginine 在 水 作用下， 生成 5-[(二氨基亚甲基)氨基]-2-氧代戊酸
  参考文献：
  名称：

  Importance of glutamate 87 and the substrate α-amine for the reaction catalyzed by d-arginine dehydrogenase

  摘要：

  Pseudomonas aeruginosa D-arginine dehydrogenaie (PaDADH) catalyzes the oxidation of b-arginine to iminoarginine, which is non-enzymatically hydrolyzed to 2-ketoarginine and ammonia. Here, sitedirected mutagenesis and pH effects were used to investigate binding and catalysis of zwitterionic and cationic substrates for the enzyme. An unprotonated group with apparent pK(a) value >= 7.9 is required for binding D-arginine or D-lysine, but not D-methionine or D-leucine. This group is E87, as suggested by its replacement with leucine. An unprotonated group with pK(a) of 9.5, which persists in the H48F and E87L variants, is required for amine oxidation with all substrates. Since Y53 and Y249 were previously ruled out, the pK(a) is assigned to the substrate alpha-NH3+ group, which previous QM/MM and K-d pH-profile demonstrated to be protonated for preferred binding to the enzyme. Lack of pH effects on the Dk(red) with D-leucine established 9.5 as the intrinsic pK(a), and D-leucine as a non-sticky substrate. D-Arginine, D-lysine and D-methionine and their corresponding iminoproducts were significantly stickier than D-leucine, as indicated by apparent pK(a) values <9.5 in both k(cat)/K-m and k(cat). Restricted proton movements in catalysis were established from hollowed k(cat) pH profiles in wild-type PaDADH with D-lysine and in the H48F and E87L enzymes with D-arginine. (C) 2015 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.abb.2015.01.017
• 作为产物：
  描述：

  D-精氨酸 在 pseudomonas aeruginosa D-arginine dehydrogenase 、 5-甲基吩嗪硫酸甲酯 作用下， 以 aq. phosphate buffer 为溶剂， 生成 Iminoarginine
  参考文献：
  名称：

  Importance of glutamate 87 and the substrate α-amine for the reaction catalyzed by d-arginine dehydrogenase

  摘要：

  Pseudomonas aeruginosa D-arginine dehydrogenaie (PaDADH) catalyzes the oxidation of b-arginine to iminoarginine, which is non-enzymatically hydrolyzed to 2-ketoarginine and ammonia. Here, sitedirected mutagenesis and pH effects were used to investigate binding and catalysis of zwitterionic and cationic substrates for the enzyme. An unprotonated group with apparent pK(a) value >= 7.9 is required for binding D-arginine or D-lysine, but not D-methionine or D-leucine. This group is E87, as suggested by its replacement with leucine. An unprotonated group with pK(a) of 9.5, which persists in the H48F and E87L variants, is required for amine oxidation with all substrates. Since Y53 and Y249 were previously ruled out, the pK(a) is assigned to the substrate alpha-NH3+ group, which previous QM/MM and K-d pH-profile demonstrated to be protonated for preferred binding to the enzyme. Lack of pH effects on the Dk(red) with D-leucine established 9.5 as the intrinsic pK(a), and D-leucine as a non-sticky substrate. D-Arginine, D-lysine and D-methionine and their corresponding iminoproducts were significantly stickier than D-leucine, as indicated by apparent pK(a) values <9.5 in both k(cat)/K-m and k(cat). Restricted proton movements in catalysis were established from hollowed k(cat) pH profiles in wild-type PaDADH with D-lysine and in the H48F and E87L enzymes with D-arginine. (C) 2015 Elsevier Inc. All rights reserved.

  DOI：

  10.1016/j.abb.2015.01.017

文献信息

• Importance of glutamate 87 and the substrate α-amine for the reaction catalyzed by d-arginine dehydrogenase
  作者：Jacob Ball、Quan V.V. Bui、Swathi Gannavaram、Giovanni Gadda

  DOI：10.1016/j.abb.2015.01.017

  日期：2015.2

  Pseudomonas aeruginosa D-arginine dehydrogenaie (PaDADH) catalyzes the oxidation of b-arginine to iminoarginine, which is non-enzymatically hydrolyzed to 2-ketoarginine and ammonia. Here, sitedirected mutagenesis and pH effects were used to investigate binding and catalysis of zwitterionic and cationic substrates for the enzyme. An unprotonated group with apparent pK(a) value >= 7.9 is required for binding D-arginine or D-lysine, but not D-methionine or D-leucine. This group is E87, as suggested by its replacement with leucine. An unprotonated group with pK(a) of 9.5, which persists in the H48F and E87L variants, is required for amine oxidation with all substrates. Since Y53 and Y249 were previously ruled out, the pK(a) is assigned to the substrate alpha-NH3+ group, which previous QM/MM and K-d pH-profile demonstrated to be protonated for preferred binding to the enzyme. Lack of pH effects on the Dk(red) with D-leucine established 9.5 as the intrinsic pK(a), and D-leucine as a non-sticky substrate. D-Arginine, D-lysine and D-methionine and their corresponding iminoproducts were significantly stickier than D-leucine, as indicated by apparent pK(a) values <9.5 in both k(cat)/K-m and k(cat). Restricted proton movements in catalysis were established from hollowed k(cat) pH profiles in wild-type PaDADH with D-lysine and in the H48F and E87L enzymes with D-arginine. (C) 2015 Elsevier Inc. All rights reserved.