2-Hydroxychromene-2-carboxylate

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 苯并吡喃
• 英文名称: 2-Hydroxychromene-2-carboxylate
• 化学式: C10H7O4-
• 分子量: 191.16
• InChiKey: LGYIZQLNYONEFJ-UHFFFAOYSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.4
• 重原子数：
  14
• 可旋转键数：
  0
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.1
• 拓扑面积：
  69.6
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为反应物：
  描述：

  2-Hydroxychromene-2-carboxylate 生成 trans-o-hydroxybenzylidenepyruvate
  参考文献：
  名称：

  Identification and functional analysis of the genes for naphthalenesulfonate catabolism by Sphingomonas xenophaga BN6

  摘要：

  BN6能够降解各种（取代）萘磺酸盐为相应的（取代）水杨酸盐。在质粒pBN6上鉴定出一个基因簇，编码了参与萘磺酸盐降解途径的多个酶。测序了含有17个ORF的16,915 bp的DNA片段。在该DNA片段上鉴定出编码萘磺酸盐途径的1,2-二羟基萘二氧化酶、2-羟基咔啉-2-羧酸异构酶和2'-羟基苯丙酮醛缩酮酶的基因，并在大肠杆菌中异源表达编码的蛋白。此外，通过插入失活法鉴定出了多组分环氧化萘磺酸盐二氧化酶的ferredoxin和ferredoxin还原酶的编码基因。鉴定出的基因通常与菲的降解菌 sp. P2或萘和联苯降解菌 F199的megaplasmid pNL1编码的酶具有最高的同源性。参与萘磺酸盐降解的 BN6基因与Sphingomonas sp. P2和S. aromaticivorans F199中先前发现的参与萘、联苯和菲降解的基因具有相同的组织形式，分布在三个不同的转录单元中。这些基因在 BN6中被ORF包围，这些ORF指定的蛋白质与移动基因元件的蛋白质具有最高的同源性。

  DOI：

  10.1099/mic.0.28783-0
• 作为产物：
  描述：

  1,2-二羟基萘 、 氧气 生成 2-Hydroxychromene-2-carboxylate 、 氢(+1)阳离子
  参考文献：
  名称：

  从降解萘磺酸的细菌中纯化和表征1,2-二羟基萘双加氧酶。

  摘要：

  从降解萘磺酸的细菌（菌株BN6）中纯化1,2-二羟基萘双加氧酶至同质。该酶需要Fe2 +才能发挥最大活性，并由八个相同的亚基组成，分子量约为33,000。NH2-末端氨基酸序列的分析显示与来自假单胞菌假单胞菌Q1的2，3-二羟基联苯双加氧酶的NH2-末端氨基酸序列高度同源（29个氨基酸中的22个）。来自菌株BN6的1,2-二羟基萘双加氧酶显示出较宽的底物特异性，还可以裂解5-，6-和7-羟基-1,2-二羟基萘，2,3-和3,4-二羟基联苯，邻苯二酚和3-甲基和4-甲基邻苯二酚。在从降解萘的细菌的细胞提取物中也发现了对羟基-1,2-二羟基萘的类似活性。

  DOI：

  10.1128/jb.173.12.3795-3802.1991

文献信息

• Purification and Some Properties of 2-Hydroxychromene-2-Carboxylate Isomerase from Naphthalenesulfonate-Assimilating Pseudomonas sp. TA-2
  作者：T. Ohmoto、T. Kinoshita、K. Moriyoshi、K. Sakai、N. Hamada、T. Ohe

  DOI：10.1093/oxfordjournals.jbchem.a022152

  日期：1998.9.1

  30 amino acid sequence had high homology with the deduced amino acid sequences of the 2HC2CA isomerase of nahD (a gene of naphthalene metabolism), pahD (a gene of naphthalene and phenanthrene metabolism), and doxJ (a gene of dibenzothiophene metabolism). The enzymatic product was a trans isomer. The isomerase activity was inhibited in the presence of monoiodoacetate or Hg2+, but not by preincubation

  从萘磺酸同化的假单胞菌sp。的无细胞提取物中纯化2-羟基亚甲基-2-羧酸异构酶。通过在DEAE-纤维素，DEAE-Toyopearl 650M，Sephadex G-75，羟基磷灰石和Mono Q上的连续柱色谱法将TA-2变为电泳均质状态。通过SDS-PAGE估算，该酶的分子量为25和27 kDa。和Superdex 200。它的N端30个氨基酸序列与nahD（萘代谢基因），pahD（萘和菲代谢基因）和doxJ（二苯并噻吩代谢基因）的2HC2CA异构酶的推导氨基酸序列具有高度同源性。 ）。酶促产物是反式异构体。在单碘乙酸盐或Hg2 +存在下，异构酶活性受到抑制，但不可与碘代乙酸盐或N-乙基马来酰亚胺预孵育。GSH充当辅因子，并在0.15 mM以上激活酶。
• Naphthalene metabolism by pseudomonads: purification and properties of 1,2-dihydroxynaphthalene oxygenase
  作者：T R Patel、E A Barnsley

  DOI：10.1128/jb.143.2.668-673.1980

  日期：1980.8

  1,2-Dihydroxynaphthalene oxygenase was purified from Pseudomonas putida NCIB 9816 grown on naphthalene as the sole source of carbon and energy. The enzyme had a subunit molecular weight of 19,000 and in a medium containing phosphate buffer, 1 mM mercaptoethanol, and 10% (vol/vol) ethanol had a native molecular weight greater than 275,000. The enzyme required Fe2+ for activity. It was inactivated slowly on standing, and inactivation was accelerated by dilution with aerated buffers and by H2O2. Bathophenanthroline sulfonate, o-phenanthroline, 8-hydroxyquinoline, and 2,2'-dipyridyl also inhibited the enzyme. The inactive enzyme was reactivated by anaerobic incubation with ferrous sulfate and ferrous ammonium sulfate. Thiol reagents and acetone, ethanol, or glycerol decreased the rate of loss of activity. The enzyme was most active with 1,2-dihydroxynaphthalene, for which the Km was 2.8 X 10(-4) M. 3-Methyl- and 4-methylcatechols were oxidized at 3 and 1.5%, respectively, of the rate of 1,2-dihydroxynaphthalene, and the Km for 3-methylcatechol was 1.5 X 10(-4) M. Purified 1,2-dihydroxynaphthalene oxygenase catalyzed the oxidation of 1,2-dihydroxynaphthalene, leading to the appearance of 2-hydroxychromene-2-carboxylic acid, but 3-methylcatechol was oxidized by this enzyme to 2-hydroxy-6-oxoheptadienoic acid. Thus, a product structurally analogous to 2-hydroxychromene-2-carboxylic acid was not observed when 3-methylcatechol was oxidized. This may indicate that 2-hydroxychromene-2-carboxylic acid results from cyclization of a ring fission product before release from the enzyme.

  1,2-二羟基萘氧化酶从生长在萘为唯一的碳源和能源的假单胞菌NCIB 9816中纯化出来。该酶的亚基分子量为19,000，在含磷酸盐缓冲液、1 mM巯基乙醇和10%(体积/体积)乙醇的培养基中，其原生分子量大于275,000。该酶需要Fe2+才能发挥活性。该酶在静置中缓慢失活，而稀释氧化缓冲液和H2O2加速失活。巴托菲南啉磺酸盐、o-菲啰啉、8-羟基喹啉和2,2'-联吡啶也能抑制该酶的活性。失活的酶可通过无氧培养与硫酸亚铁和铵铁硫酸盐再次活化。巯基试剂和丙酮、乙醇或甘油可降低酶活性的丧失速率。该酶在1,2-二羟基萘的作用下最为活跃，其Km值为2.8×10(-4) M。3-甲基和4-甲基邻苯二酚的氧化速率分别为1.5%和3%的1,2-二羟基萘的速率，3-甲基邻苯二酚的Km值为1.5×10(-4) M。纯化的1,2-二羟基萘氧化酶催化1,2-二羟基萘的氧化，产生2-羟基色酮-2-羧酸，但该酶将3-甲基邻苯二酚氧化为2-羟基-6-氧代庚二烯酸。因此，在氧化3-甲基邻苯二酚时未观察到结构类似于2-羟基色酮-2-羧酸的产物，这可能表明在释放酶之前，环裂解产物发生环化反应形成2-羟基色酮-2-羧酸。
• 2-Hydroxychromene-2-carboxylic Acid Isomerase:  A Kappa Class Glutathione Transferase from <i>Pseudomonas putida</i>^,^,
  作者：Lawrence C. Thompson、Jane E. Ladner、Simona G. Codreanu、Joel Harp、Gary L. Gilliland、Richard N. Armstrong

  DOI：10.1021/bi700356u

  日期：2007.6.1

  The enzyme 2-hydroxychromene-2-carboxylic acid (HCCA) isomerase catalyzes the glutathione (GSH)-dependent interconversion (Keq = 1.5) of HCCA and trans-o-hydroxybenzylidene pyruvic acid (tHBPA) in the naphthalene catabolic pathway of Pseudomonas putida. The dimeric protein binds one molecule of GSH very tightly (Kd approximately 5 nM) and a second molecule of GSH with much lower affinity (Kd approximately 2 to 11 microM). The enzyme is unstable in the absence of GSH. The turnover number in the forward direction (47 s(-1) at 25 degrees C) greatly exceeds off rates for GSH (koff approximately 10(-3) to 10(-2) s(-1) at 10 degrees C), suggesting that GSH acts as a tightly bound cofactor in the reaction. The crystal structure of the enzyme at 1.7 A resolution reveals that the isomerase is closely related to class kappa GSH transferases. Diffraction quality crystals could only be obtained in the presence of GSH and HCCA/tHBPA. Clear electron density is seen for GSH. Electron density for the organic substrates is located near the GSH and is best modeled to include both HCCA and tHBPA at occupancies of 0.5 for each. Although there is no electron density connecting the sulfur of GSH to the organic substrates, the sulfur is located very close (2.78 A) to C7 of HCCA. Taken together, the results suggest that the isomerization reaction involves a short-lived covalent adduct between the sulfur of GSH and C7 of the substrate.