L-cysteine sulfinate | 78543-51-8

• 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-cysteine sulfinate
• 英文别名: cysteine sulfinate；L-cysteine-S-dioxide；(2R)-2-amino-3-hydroxy-3-oxopropane-1-sulfinate
• CAS: 78543-51-8
• 化学式: C₃H₆NO₄S
• 分子量: 152.151
• InChiKey: ADVPTQAUNPRNPO-REOHCLBHSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -4.1
• 重原子数：
  9
• 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：
  127
• 氢给体数：
  1
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  L-cysteine sulfinate 、 氢(+1)阳离子 生成 二氧化碳 、 亚牛磺酸
  参考文献：
  名称：

  Purification and Characterization of the First Archaeal Glutamate Decarboxylase fromPyrococcus horikoshii

  摘要：

  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。

  DOI：

  10.1271/bbb.80583
• 作为产物：
  描述：

  L-半胱氨酸 、 L-组氨酸 在 3,3,3-膦三基三丙酸 、 recombinant OvoA protein 、 抗坏血酸 、 氧气 作用下， 以 aq. buffer 为溶剂， 生成 S-(5-histidyl)cysteine sulfoxide 、 L-cysteine sulfinate
  参考文献：
  名称：

  Cysteine Oxidation Reactions Catalyzed by a Mononuclear Non-heme Iron Enzyme (OvoA) in Ovothiol Biosynthesis

  摘要：

  OvoA in ovothiol biosynthesis is a mononuclear non-heme iron enzyme catalyzing the oxidative coupling between histidine and cysteine. It can also catalyze the oxidative coupling between hercynine and cysteine, yet with a different regio-selectivity. Due to the potential application of this reaction for industrial ergothioneine production, in this study, we systematically characterized OvoA by a combination of three different assays. Our studies revealed that OvoA can also catalyze the oxidation of cysteine to either cysteine sulfinic acid or cystine. Remarkably, these OvoA-catalyzed reactions can be systematically modulated by a slight modification of one of its substrates, histidine.

  DOI：

  10.1021/ol5005438

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。
• 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，
• Structure and mechanism of mouse cysteine dioxygenase
  作者：Jason G. McCoy、Lucas J. Bailey、Eduard Bitto、Craig A. Bingman、David J. Aceti、Brian G. Fox、George N. Phillips

  DOI：10.1073/pnas.0509262103

  日期：2006.2.28

  Cysteine dioxygenase (CDO) catalyzes the oxidation of l-cysteine to cysteine sulfinic acid. Deficiencies in this enzyme have been linked to autoimmune diseases and neurological disorders. The x-ray crystal structure of CDO from Mus musculus was solved to a nominal resolution of 1.75 Angstroms. The sequence is 91% identical to that of a human homolog. The structure reveals that CDO adopts the typical

  半胱氨酸双加氧酶（CDO）催化L-半胱氨酸氧化为半胱氨酸亚磺酸。该酶的缺乏与自身免疫性疾病和神经系统疾病有关。将小家鼠的CDO的X射线晶体结构解析为1.75埃的标称分辨率。该序列与人类同源物的序列具有91％的同一性。该结构表明，CDO采用了铜杯超家族的典型β-桶折叠。His-86，-88和-140的NE2原子提供金属结合位点。该结构进一步揭示了Cys-93和Tyr-157的侧链之间的共价键，其半胱氨酸仅在真核蛋白中保守。金属分析表明，重组酶含有铁，镍和锌的混合物，铁含量的增加与催化活性的增加有关。
• Cysteine Sulfinate Desulfinase, a NIFS-like Protein ofEscherichia coli with Selenocysteine Lyase and Cysteine Desulfurase Activities
  作者：Hisaaki Mihara、Tatsuo Kurihara、Tohru Yoshimura、Kenji Soda、Nobuyoshi Esaki

  DOI：10.1074/jbc.272.36.22417

  日期：1997.9

  Selenocysteine lyase (EC 4.4.1.16) exclusively decomposes selenocysteine to alanine and elemental selenium, whereas cysteine desulfurase (NIFS protein) of Azotobacter vinelandii acts indiscriminately on both cysteine and selenocysteine to produce elemental sulfur and selenium respectively, and alanine. These proteins exhibit some sequence homology, The Escherichia coli genome contains three genes with sequence homology to nifS. We have cloned the gene mapped at 63.4 min in the chromosome and have expressed, purified to homogeneity, and characterized the gene product, The enzyme comprises two identical subunits with 401 amino acid residues (M-r 43,238) and contains pyridoxal 5'-phosphate as a coenzyme. The enzyme catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, Because L-cysteine sulfinic acid was desulfinated to form L-alanine as the preferred substrate, we have named this new enzyme cysteine sulfinate desulfinase. Mutant enzymes having alanine substituted for each of the four cysteinyl residues (Cys-100, Cys-176, Cys-323, and Cys-358) were all active, Cys-358 corresponds to Cys-325 of A. vinelandii NIFS, which is conserved among all NIFS-like proteins and catalytically essential (Zheng, L., White, R. H., Cash, V. L., and Dean, D. R. (1994) Biochemistry 33, 4714-4720), is not required for cysteine sulfinate desulfinase. Thus, the enzyme is distinct from A. vinelandii NIFS in this respect.
• Crystal Structure of Mammalian Cysteine Dioxygenase
  作者：Chad R. Simmons、Qun Liu、Qingqiu Huang、Quan Hao、Tadhg P. Begley、P. Andrew Karplus、Martha H. Stipanuk

  DOI：10.1074/jbc.m601555200

  日期：2006.7

  Cysteine dioxygenase is a mononuclear iron-dependent enzyme responsible for the oxidation of cysteine with molecular oxygen to form cysteine sulfinate. This reaction commits cysteine to either catabolism to sulfate and pyruvate or the taurine biosynthetic pathway. Cysteine dioxygenase is a member of the cupin superfamily of proteins. The crystal structure of recombinant rat cysteine dioxygenase has been determined to 1.5-A resolution, and these results confirm the canonical cupin beta-sandwich fold and the rare cysteinyltyrosine intramolecular cross-link (between Cys(93) and Tyr(157)) seen in the recently reported murine cysteine dioxygenase structure. In contrast to the catalytically inactive mononuclear Ni(II) metallocenter present in the murine structure, crystallization of a catalytically competent preparation of rat cysteine dioxygenase revealed a novel tetrahedrally coordinated mononuclear iron center involving three histidines (His(86), His(88), and His(140)) and a water molecule. Attempts to acquire a structure with bound ligand using either cocrystallization or soaking crystals with cysteine revealed the formation of a mixed disulfide involving Cys(164) near the active site, which may explain previously observed substrate inhibition. This work provides a framework for understanding the molecular mechanisms involved in thiol dioxygenation and sets the stage for exploration of the chemistry of both the novel mononuclear iron center and the catalytic role of the cysteinyl-tyrosine linkage.