L-cysteic acid

• 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: L-cysteic acid
• 英文别名: (2R)-2-amino-3-sulfopropanoate
• 化学式: C₃H₅NO₅S*2H
• 分子量: 169.158
• InChiKey: XVOYSCVBGLVSOL-REOHCLBHSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -3.9
• 重原子数：
  10
• 可旋转键数：
  1
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  133
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-cysteic acid 、 三丁基氧化锡 以 乙醇 为溶剂， 以66%的产率得到(n-Bu3Sn)2 L-cysteicate*2H2O
  参考文献：
  名称：

  Mössbauer spectra of organotin amino-acid and glutathione derivatives

  摘要：

  DOI：

  10.1016/s0022-328x(00)83515-9
• 作为产物：
  描述：

  L-半胱氨酸 、 三氧化硫 生成 硫化氢 、 L-cysteic acid
  参考文献：
  名称：

  半胱氨酸裂解酶催化鸡胚卵黄囊中的反应。

  摘要：

  DOI：

  10.1016/0005-2744(69)90174-0

文献信息

• Purification and Characterization of the First Archaeal Glutamate Decarboxylase from<i>Pyrococcus horikoshii</i>
  作者：Han-Woo KIM、Yasuhiro KASHIMA、Kazuhiko ISHIKAWA、Naoko YAMANO

  DOI：10.1271/bbb.80583

  日期：2009.1.23

  Glutamate decarboxylase (GAD) from the archaeon Pyrococcus horikoshii was successfully expressed and purified, with the aim of developing a hyperthermostable GAD for industrial applications. Its biochemical properties were different from those reported for other GADs. The enzyme had broad substrate specificity, and its optimum pH and temperature were pH 8.0 and >97 °C.

  来自古菌株Pyrococcus horikoshii的谷氨酸脱羧酶(GAD)成功表达并纯化，旨在开发用于工业应用的超热稳定GAD。其生化特性与之前报道的其他GAD不同。该酶具有广泛的底物特异性，其最适pH和温度分别为pH 8.0和>97 °C。
• <scp>L</scp>-Cysteate sulpho-lyase, a widespread pyridoxal 5′-phosphate-coupled desulphonative enzyme purified from <i>Silicibacter pomeroyi</i> DSS-3T
  作者：Karin Denger、Theo H. M. Smits、Alasdair M. Cook

  DOI：10.1042/bj20051311

  日期：2006.3.15

  Quantitative utilization of L-cysteate (2-amino-3-sulphopropionate) as the sole source of carbon and energy for growth of the aerobic, marine bacterium Silicibacter pomeroyi DSS-3T was observed. The sulphonate moiety was recovered in the medium largely as sulphite, and the appropriate amount of the ammonium ion was also observed. Genes [suyAB (3-sulpholactate sulpho-lyase)] encoding the known desulphonation reaction in cysteate degradation were absent from the genome, but a homologue of a putative sulphate exporter gene (suyZ) was found, and its neighbour, annotated as a D-cysteine desulphhydrase, was postulated to encode pyridoxal 5′-phosphate-coupled L-cysteate sulpho-lyase (CuyA), a novel enzyme. Inducible CuyA was detected in cysteate-grown cells. The enzyme released equimolar pyruvate, sulphite and the ammonium ion from L-cysteate and was purified to homogeneity by anion-exchange, hydrophobic-interaction and gel-filtration chromatography. The N-terminal amino acid sequence of this 39-kDa subunit confirmed the identification of the cuyA gene. The native enzyme was soluble and homomultimeric. The Km-value for L-cysteate was high (11.7 mM) and the enzyme also catalysed the D-cysteine desulphhydrase reaction. The gene cuyZ, encoding the putative sulphite exporter, was co-transcribed with cuyA. Sulphite was exported despite the presence of a ferricyanide-coupled sulphite dehydrogenase. CuyA was found in many bacteria that utilize cysteate.

  观察到需氧海洋细菌波美拉尼亚硅杆菌（Silicibacter pomeroyi DSS-3T）定量利用 L-半胱氨酸（2-氨基-3-磺丙酸）作为生长的唯一碳源和能量来源。培养基中的磺酸盐主要以亚硫酸盐的形式回收，同时还观察到适量的铵离子。基因组中没有编码半胱氨酸降解过程中已知的脱硫反应的基因[suyAB（3-磺酸内酯磺酸水解酶）]，但发现了一个推测的硫酸盐出口基因（suyZ）的同源物、其邻近基因（注释为 D-半胱氨酸脱硫水解酶）被推测编码吡哆醛-5′-磷酸耦合 L-半胱氨酸硫酸水解酶（CuyA），这是一种新型酶。在半胱氨酸生长细胞中检测到了可诱导的 CuyA。该酶从 L-半胱氨酸中释放出等摩尔的丙酮酸、亚硫酸盐和铵离子，并通过阴离子交换、疏水相互作用和凝胶过滤色谱法纯化至均一。这种 39 kDa 亚基的 N 端氨基酸序列证实了 cuyA 基因的鉴定。原生酶是可溶的、同源的。L 型半胱氨酸的 Km 值很高（11.7 mM），该酶还能催化 D 型半胱氨酸脱硫水解酶反应。编码假定亚硫酸盐输出器的基因 cuyZ 与 cuyA 是共转录的。尽管存在与亚硫酸铁耦合的亚硫酸脱氢酶，但亚硫酸仍被输出。在许多利用半胱氨酸的细菌中都发现了 CuyA。
• Rat liver cysteine sulfinate decarboxylase: purification, new appraisal of the molecular weight and determination of catalytic properties
  作者：Marie-Christine Guion-Rain、Christiane Portemer、Fernande Chatagner

  DOI：10.1016/0005-2744(75)90115-1

  日期：1975.3

  Rat liver cystein sulfinate decarboxylase (L-cystein sulfinate carboxylase) was purified approximately 500-fold. By cellulose acetate and polyacrylamide gel electrophoresis or by analytical ultracentrifugation, the purified enzyme appears to be nearly homogeneous. The Stokes radius (3.4 nm) and sedimentation coefficient (6.5 S) were determined. The molecular weight, calculated and experimentally estimated

  将大鼠肝半胱氨酸亚磺酸脱羧酶（L-半胱氨酸亚磺酸羧化酶）纯化约500倍。通过乙酸纤维素和聚丙烯酰胺凝胶电泳或通过分析超速离心，纯化的酶似乎几乎是均质的。测定斯托克斯半径（3.4nm）和沉降系数（6.5S）。计算和实验估算的分子量约为10万，该酶由分子量为55 000的两个相同的亚基组成。证明了吡ido醛磷酸盐作为辅酶的作用，并研究了活性所需的游离巯基的需求。强调了天然纯半胱氨酸亚磺酸脱羧酶也能使半胱氨酸脱羧的能力：因此，我们得出的结论是，在大鼠肝脏中，单一蛋白质可催化两种反应，
• Convergent evolution of coenzyme M biosynthesis in the Methanosarcinales: cysteate synthase evolved from an ancestral threonine synthase
  作者：David E. Graham、Stephanie M. Taylor、Rachel Z. Wolf、Seema C. Namboori

  DOI：10.1042/bj20090999

  日期：2009.12.15

  The euryarchaeon Methanosarcina acetivorans has no homologues of the first three enzymes that produce the essential methanogenic coenzyme M (2-mercaptoethanesulfonate) in Methanocaldococcus jannaschii. A single M. acetivorans gene was heterologously expressed to produce a functional sulfopyruvate decarboxylase protein, the fourth canonical enzyme in this biosynthetic pathway. An adjacent gene, at locus MA3297, encodes one of the organism's two threonine synthase homologues. When both paralogues from this organism were expressed in an Escherichia coli threonine synthase mutant, the MA1610 gene complemented the thrC mutation, whereas the MA3297 gene did not. Both PLP (pyridoxal 5′-phosphate)-dependent proteins were heterologously expressed and purified, but only the MA1610 protein catalysed the canonical threonine synthase reaction. The MA3297 protein specifically catalysed a new β-replacement reaction that converted L-phosphoserine and sulfite into L-cysteate and inorganic phosphate. This oxygen-independent mode of sulfonate biosynthesis exploits the facile nucleophilic addition of sulfite to an α,β-unsaturated intermediate (PLP-bound dehydroalanine). An amino acid sequence comparison indicates that cysteate synthase evolved from an ancestral threonine synthase through gene duplication, and the remodelling of active site loop regions by amino acid insertion and substitutions. The cysteate product can be converted into sulfopyruvate by an aspartate aminotransferase enzyme, establishing a new convergent pathway for coenzyme M biosynthesis that appears to function in members of the orders Methanosarcinales and Methanomicrobiales. These differences in coenzyme M biosynthesis afford the opportunity to develop methanogen inhibitors that discriminate between the classes of methanogenic archaea.

  极毛石龙子 Methanosarcina acetivorans 没有同源的前三种酶，而这三种酶都是产生甲烷生成辅酶 M（2-巯基乙烷磺酸盐）的关键酶。通过异源表达 M. acetivorans 的单个基因，可产生功能性硫基丙酮酸脱羧酶蛋白，这是该生物合成途径中的第四种典型酶。相邻基因（位于 MA3297 位点）编码该生物体两个苏氨酸合成酶同源物之一。当在大肠杆菌苏氨酸合成酶突变体中表达该生物的这两个同源基因时，MA1610 基因能补充 thrC 突变，而 MA3297 基因则不能。两种依赖于 PLP（5′-磷酸吡哆醛）的蛋白都得到了异源表达和纯化，但只有 MA1610 蛋白催化了典型的苏氨酸合成酶反应。MA3297 蛋白特异性地催化了一种新的β置换反应，将 L-磷酸丝氨酸和亚硫酸盐转化为 L-半胱氨酸和无机磷酸盐。这种不依赖氧的磺酸盐生物合成模式利用了亚硫酸盐与α,β-不饱和中间体（与 PLP 结合的脱氢丙氨酸）的亲核加成反应。氨基酸序列比较表明，半胱氨酸合成酶是从祖先的苏氨酸合成酶通过基因复制、氨基酸插入和替换重塑活性位点环区进化而来的。半胱氨酸产物可通过天门冬氨酸氨基转移酶转化为硫代丙酮酸，从而建立了一条新的辅酶 M 生物合成汇合途径，该途径似乎在甲烷肉碱目和甲烷微生物目中发挥作用。辅酶 M 生物合成过程中的这些差异为开发能够区分甲烷古细菌类别的甲烷菌抑制剂提供了机会。