N-hydroxyoxamate | 5164-16-9

• 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: N-hydroxyoxamate
• 英文别名: oxalomonohydroxamic acid；Oxalomonohydroxamsaeure；N-hydroxyoxamic acid；2-(hydroxyamino)-2-oxoacetic acid
• CAS: 5164-16-9
• 化学式: C₂H₃NO₄
• mdl: MFCD20617208
• 分子量: 105.05
• InChiKey: CSXHUONYHRDYGM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  7
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.0
• 拓扑面积：
  86.6
• 氢给体数：
  3
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  N-hydroxyoxamate 在 盐酸 、 溴甲酚绿 、 sodium cyanoborohydride 作用下， 以 甲醇 为溶剂， 反应 3.0h， 以33%的产率得到N-羟基甘氨酸
  参考文献：
  名称：

  Does N-hydroxyglycine inhibit plant and fungal laccases?

  摘要：

  The effect of N-hydroxyglycine on the oxidation of substrates, syringaldazine, tolidine, 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol, by fungal and plant laccases was examined. At mu M concentrations, N-hydroxyglycine decolorized solutions of substrates oxidized enzymatically by laccase or chemically by sodium periodate. This discoloration, or bleaching, could be mistaken for inhibition of laccase activity if N-hydroxyglycine was added to assays for laccase that monitored colored products. N-hydroxyglycine also affected oxygen consumption assays when some of these substrates were oxidized enzymatically or chemically. Spectral scans of the products formed during enzymatic or chemical oxidation of the substrates indicated that addition of N-hydroxyglycine caused a general decrease in absorption. Except for 2,6-dimethoxyphenol, no formation of new absorption peaks was noted. These results suggest that N-hydroxyglycine may not be a "classical" enzyme inhibitor of laccase, but that this compound interferes with both spectrophotometric and oxygen uptake enzyme assays for laccase. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0031-9422(99)00302-7
• 作为产物：
  描述：

  N-Hydroxy-oxalamic acid tert-butyl ester 在 三氟乙酸 作用下， 以 二氯甲烷 为溶剂， 反应 0.25h， 以95%的产率得到N-hydroxyoxamate
  参考文献：
  名称：

  O-Alkyl Hydroxamates as Metaphors of Enzyme-Bound Enolate Intermediates in Hydroxy Acid Dehydrogenases. Inhibitors of Isopropylmalate Dehydrogenase, Isocitrate Dehydrogenase, and Tartrate Dehydrogenase¹

  摘要：

  The inhibition of Thermus thermophilus isopropylmalate dehydrogenase by O-methyl oxalohydroxamate was studied for comparison to earlier results of Schloss with the Salmonella enzyme. It is a fairly potent (1.2 mu M), slow-binding, uncompetitive inhibitor against isopropylmalate and is far superior to an oxamide (25 mM K-i competitive) that is isosteric with the ketoisocaproate product of the enzyme. This improvement in inhibition was attributed to its increased NH acidity, which presumably is due to the inductive effect of the hydroxylamine oxygen. This principle was extended to the structurally homologous enzyme isocitrate dehydrogenase from E. coli, for which the compound O-(carboxymethyl) oxalohydroxamate is a 30 nM inhibitor, uncompetitive against isocitrate. The pH dependence of its inhibition supports the idea that it is bound to the enzyme in the anionic form. Another recently discovered homologous enzyme, tartrate dehydrogenase from Pseudomonas putida, was studied with oxalylhydroxamate. It has a relatively low affinity for the enzyme, though it is superior to tartrate. On the basis of these leads, squaric hydroxamates with increased acidity compared to squaric amides directed toward two of these enzymes were prepared, and they also show increased inhibitory potency, though not approaching the nanomolar levels of the oxalylhydroxamates.

  DOI：

  10.1021/jo952090+

文献信息

• Synthesis of Some Hydroxamic Acids. Reactivity with Isopropyl Methylphosphonofluoridate (GB)
  作者：G. F. ENDRES、JOSEPH EPSTEIN

  DOI：10.1021/jo01092a027

  日期：1959.10
• Dimroth; Dienstbach, Chemische Berichte, 1908, vol. 41, p. 4080
  作者：Dimroth、Dienstbach

  DOI：——

  日期：——
• de Paolini; Carbone, Gazzetta Chimica Italiana, 1930, vol. 60, p. 263
  作者：de Paolini、Carbone

  DOI：——

  日期：——
• <i>O</i>-Alkyl Hydroxamates as Metaphors of Enzyme-Bound Enolate Intermediates in Hydroxy Acid Dehydrogenases. Inhibitors of Isopropylmalate Dehydrogenase, Isocitrate Dehydrogenase, and Tartrate Dehydrogenase¹
  作者：Michael C. Pirrung、Hyunsoo Han、Jrlung Chen

  DOI：10.1021/jo952090+

  日期：1996.1.1

  The inhibition of Thermus thermophilus isopropylmalate dehydrogenase by O-methyl oxalohydroxamate was studied for comparison to earlier results of Schloss with the Salmonella enzyme. It is a fairly potent (1.2 mu M), slow-binding, uncompetitive inhibitor against isopropylmalate and is far superior to an oxamide (25 mM K-i competitive) that is isosteric with the ketoisocaproate product of the enzyme. This improvement in inhibition was attributed to its increased NH acidity, which presumably is due to the inductive effect of the hydroxylamine oxygen. This principle was extended to the structurally homologous enzyme isocitrate dehydrogenase from E. coli, for which the compound O-(carboxymethyl) oxalohydroxamate is a 30 nM inhibitor, uncompetitive against isocitrate. The pH dependence of its inhibition supports the idea that it is bound to the enzyme in the anionic form. Another recently discovered homologous enzyme, tartrate dehydrogenase from Pseudomonas putida, was studied with oxalylhydroxamate. It has a relatively low affinity for the enzyme, though it is superior to tartrate. On the basis of these leads, squaric hydroxamates with increased acidity compared to squaric amides directed toward two of these enzymes were prepared, and they also show increased inhibitory potency, though not approaching the nanomolar levels of the oxalylhydroxamates.
• Does N-hydroxyglycine inhibit plant and fungal laccases?
  作者：Jingming Zhang、Richard Kjonaas、William H. Flurkey

  DOI：10.1016/s0031-9422(99)00302-7

  日期：1999.11

  The effect of N-hydroxyglycine on the oxidation of substrates, syringaldazine, tolidine, 2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol, by fungal and plant laccases was examined. At mu M concentrations, N-hydroxyglycine decolorized solutions of substrates oxidized enzymatically by laccase or chemically by sodium periodate. This discoloration, or bleaching, could be mistaken for inhibition of laccase activity if N-hydroxyglycine was added to assays for laccase that monitored colored products. N-hydroxyglycine also affected oxygen consumption assays when some of these substrates were oxidized enzymatically or chemically. Spectral scans of the products formed during enzymatic or chemical oxidation of the substrates indicated that addition of N-hydroxyglycine caused a general decrease in absorption. Except for 2,6-dimethoxyphenol, no formation of new absorption peaks was noted. These results suggest that N-hydroxyglycine may not be a "classical" enzyme inhibitor of laccase, but that this compound interferes with both spectrophotometric and oxygen uptake enzyme assays for laccase. (C) 1999 Elsevier Science Ltd. All rights reserved.