maleylacetone | 40609-69-6

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 酮酸及其衍生物
• 英文名称: maleylacetone
• 英文别名: Maleylaceton；(Z)-4,6-dioxohept-2-enoic acid
• CAS: 40609-69-6
• 化学式: C₇H₈O₄
• 分子量: 156.138
• InChiKey: MQVQZTWTXUPFFC-IHWYPQMZSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -0.4
• 重原子数：
  11
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.29
• 拓扑面积：
  71.4
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  maleylacetone 在 human glutathione transferase zeta 1c-1c 作用下， 以 phosphate buffer 为溶剂， 反应 0.5h， 生成 fumarylacetone
  参考文献：
  名称：

  马来酰丙酮和富马酰丙酮使人谷胱甘肽转移酶Zeta（hGSTZ1-1）烷基化和失活。

  摘要：

  谷胱甘肽转移酶ζ（GSTZ1-1）分别催化顺丁烯二酰乙酰乙酸酯或顺丁烯二酰丙酮（MA）顺式-反式异构化为富马酰乙酰乙酸酯或富马酰丙酮（FA）。GSTZ1-1还催化各种α-卤代酸（包括二氯乙酸）的谷胱甘肽依赖性生物转化。这项研究的目的是研究MA和FA使hGSTZ1-1失活的机制，并确定在存在和不存在谷胱甘肽的情况下MA和FA对hGSTZ1-1的共价修饰。MA和FA（0.01-1 mM）以浓度和时间依赖性方式灭活所有hGSTZ1-1多态性变体，并且谷胱甘肽阻止了这种失活。hGSTZ1c-1c的C16A突变体被MA和FA部分灭活。电喷雾电离串联质谱法和hGSTZ1多态性变体的胰蛋白酶消化物的SALSA（光谱分析评分算法）分析显示，hGSTZ1-1的活性位点（SSCSWR）和C端（LLVLEAFQVSHPCR）半胱氨酸残基已被MA和Mg共价修饰。 F A。MA和FA的加合导致修饰肽离子及其MS-M

  DOI：

  10.1021/tx025503s

文献信息

• Kinetics of the Biotransformation of Maleylacetone and Chlorofluoroacetic Acid by Polymorphic Variants of Human Glutathione Transferase Zeta (hGSTZ1-1)
  作者：Hoffman B. M. Lantum、Philip G. Board、M. W. Anders

  DOI：10.1021/tx010095y

  日期：2002.7.1

  Glutathione transferase zeta (GSTZ1-1) catalyzes the cis-trans isomerization of maleylacetoacetate and the biotransformation of a range of alpha-haloacids. The objective of this study was to determine the kinetics of the biotransformation of maleylacetone (MA), an analogue of the natural substrate maleylacetoacetate, and chlorofluoroacetic acid (CFA) by polymorphic variants of recombinant hGSTZ1-1. The k(cat) of the four variants of hGSTZ1-1 with MA as the substrate followed the order: 1c-1c > 1b-1b > 1d-1d > 1a-1a whereas the kcat for the biotransformation of CFA followed the order: similar to1a-1a > 1b-1b 1c-1c similar to 1d-1d. The turnover rates of Nu were much higher than those of CFA for each variant and ranged from 22-fold (1a-1a) to 980-fold differences (1c-1c). The catalytic efficiencies of hGSTZ1-1 variants with MA as the substrate were much greater than those with CFA as the substrate, but little difference among the polymorphic variants was observed. MA was a mixed inhibitor of all variants with CFA as substrate: the mean competitive inhibition constant (K-ic(MA)) for all variants was about 100 muM, and the mean uncompetitive inhibition constant (K-iu(MA)) was about 201 muM. Hence, MA and alpha-haloacids apparently compete for the same active site on the enzyme. DCA-induced inactivation of the four variants showed that the inactivated enzymes show markedly reduced isomerase activities. The residual activities were different for each variant: 1a-1a (12%) > 1b-1b similar to 1c-1c similar to 1d-1d (<5%). This is the first kinetic analysis of polymorphic variants of hGSTZ1-1, and the similarity of the kinetic constants for hGSTZ1-1 variants with either MA or CFA as substrates indicates that few differences in DCA-induced perturbations of tyrosine metabolism would likely be observed in humans.
• Mechanism of cis-trans isomerization about carbon-carbon double bonds catalyzed by silver(I)
  作者：Richard A. Johnson、Stanley. Seltzer

  DOI：10.1021/ja00798a042

  日期：1973.8
• Alkylation and Inactivation of Human Glutathione Transferase Zeta (hGSTZ1-1) by Maleylacetone and Fumarylacetone
  作者：Hoffman B. M. Lantum、Daniel C. Liebler、Philip G. Board、M. W. Anders

  DOI：10.1021/tx025503s

  日期：2002.5.1

  variants were incubated with MA or FA in the presence of S-methyl glutathione. These data indicate that MA and FA are substrate and product inactivators of hGSTZ1-1 and covalently modify hGSTZ1-1 at the active-site cysteine residue in the absence of glutathione. The observation that inactivation was blocked by glutathione indicates that binding of glutathione to the active site prevents reaction of MA

  谷胱甘肽转移酶ζ（GSTZ1-1）分别催化顺丁烯二酰乙酰乙酸酯或顺丁烯二酰丙酮（MA）顺式-反式异构化为富马酰乙酰乙酸酯或富马酰丙酮（FA）。GSTZ1-1还催化各种α-卤代酸（包括二氯乙酸）的谷胱甘肽依赖性生物转化。这项研究的目的是研究MA和FA使hGSTZ1-1失活的机制，并确定在存在和不存在谷胱甘肽的情况下MA和FA对hGSTZ1-1的共价修饰。MA和FA（0.01-1 mM）以浓度和时间依赖性方式灭活所有hGSTZ1-1多态性变体，并且谷胱甘肽阻止了这种失活。hGSTZ1c-1c的C16A突变体被MA和FA部分灭活。电喷雾电离串联质谱法和hGSTZ1多态性变体的胰蛋白酶消化物的SALSA（光谱分析评分算法）分析显示，hGSTZ1-1的活性位点（SSCSWR）和C端（LLVLEAFQVSHPCR）半胱氨酸残基已被MA和Mg共价修饰。 F A。MA和FA的加合导致修饰肽离子及其MS-M