nitric-oxide synthase (NADPH) | 125978-95-2

• 物质功能分类: 生物化工 - 抗体
• 分子结构分类: 氧化还原酶 - 作用于配对供体，掺入或还原分子氧 - 以 NADH 或 NADPH 作为供体，并将一个氧原子加入另一个供体中
• 英文名称: nitric-oxide synthase (NADPH)
• 英文别名: NOS (gene name)；nitric oxide synthetase (ambiguous)；endothelium-derived relaxation factor-forming enzyme；endothelium-derived relaxing factor synthase；NO synthase (ambiguous)；NADPH-diaphorase (ambiguous)；neuronal nitric oxide synthase
• CAS: 125978-95-2

反应信息

• 作为试剂：
  描述：

  (2S)-2-氨基-5-[(N'-丙-2-烯基甲脒基)氨基]戊酸 在 nitric-oxide synthase (NADPH) 还原型辅酶II(NADPH)四钠盐 、 calcium chloride 、 calmodulin 作用下， 生成 L-瓜氨酸 、 丙烯醛
  参考文献：
  名称：

  Deuterium isotope effects and product studies for the oxidation of N ω -allyl- l -arginine and N ω -allyl- N ω -hydroxy- l -arginine by neuronal nitric oxide synthase

  摘要：

  The nitric oxide synthases (NOS), which require heme, tetrahydrobiopterin, FMN, FAD, and NADPH, catalyze the O-2-dependent conversion of L-arginine to L-citrulline and nitric oxide. N-omega-Allyl-L-arginine, a mechanism-based inactivator of neuronal NOS, also is a substrate, producing L-arginine, acrolein, and H2O (Zhang, H. Q., Dixon, R. P.; Marletta, R I. A.; Nikolic, D.; Van Breemen, R.; Silverman, R. B. J. Am. Chem. SOC. 1997, 119, 10888). Two possible mechanisms for this turnover an proposed, one initiated by allyl C-I-I bond cleavage and the other by guanidino N-H cleavage, and these mechanisms are investigated with the use of N omega-allyl-L-arginine (1), N-omega-[1,1-H-2(2)]allyl-L-arginine (7), N-omega-allyl-L-hydroxy-L-alginine (2) and N-omega-[1,1-H-2(2)]allyl-N-omega-hydroxy-L-arginine (8) as substrates. Significant isotope effects on the two kinetic parameters, k(cat) and k(cat)/k(m) are observed in case of 1 and 7 during turnover, but not with 2 and 8. No kinetic isotope effects are observed for either compound in their role as inactivators. These results support a mechanism involving initial CH bond cleavage of N-omega-allyl-L-arginine followed by hydroxylation and beakdown to products. (C) 2000 Published by Elsevier Science Ltd.

  DOI：

  10.1016/s0968-0896(00)00154-1