(S)-2-chloropropanoate

• 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: (S)-2-chloropropanoate
• 英文别名: (2S)-2-chloropropanoate
• 化学式: C3H4ClO2-
• 分子量: 107.51
• InChiKey: GAWAYYRQGQZKCR-REOHCLBHSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  1.5
• 重原子数：
  6
• 可旋转键数：
  0
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.67
• 拓扑面积：
  40.1
• 氢给体数：
  0
• 氢受体数：
  2

反应信息

• 作为反应物：
  描述：

  (S)-2-chloropropanoate 、 NADP⁺ 生成 α-chloroacrylate 、 氢(+1)阳离子 、 NADPH(4-)
  参考文献：
  名称：

  2-卤代丙烯酸酯还原酶，一种中链脱氢酶/还原酶超家族的新型酶，可催化不饱和有机卤素化合物的碳-碳双键的还原。

  摘要：

  土壤细菌，伯克霍尔德氏菌。WS以2-氯丙烯酸酯为唯一碳源生长。为了鉴定代谢2-氯丙烯酸酯的酶，我们对2-氯丙烯酸酯和乳酸生长的细菌细胞中的蛋白质进行了比较二维凝胶电泳。结果，我们发现，当细胞在2-氯丙烯酸酯上生长时，可诱导合成名为CAA43的蛋白质。克隆了CAA43基因并显示出编码333个氨基酸残基的蛋白质（M（r）35,788），该蛋白质与来自大肠杆菌的NADPH依赖性醌氧化还原酶具有显着的序列相似性（38.2％同一性）。CAA43在大肠杆菌中过量产生，并纯化至均质。纯化的蛋白质催化了2-氯丙烯酸酯的碳-碳双键的NADPH依赖性还原反应，生成（S）-2-氯丙酸酯，在伯克霍尔德氏菌中，它可能被（S）-2-卤代酸脱卤酶进一步代谢为（R）-乳酸。WS。NADH不能用作还原剂。尽管序列与醌氧化还原酶相似，但CAA43并未作用于1,4-苯醌和1,4-萘醌。2-氯丙烯酸酯类似物，例如丙烯酸酯和甲基丙

  DOI：

  10.1074/jbc.m414605200

文献信息

• Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene
  作者：J van der Ploeg、G van Hall、D B Janssen

  DOI：10.1128/jb.173.24.7925-7933.1991

  日期：1991.12

  The haloacid dehalogenase of the 1,2-dichloroethane-utilizing bacterium Xanthobacter autotrophicus GJ10 was purified from a mutant with an eightfold increase in expression of the enzyme. The mutant was obtained by selecting for enhanced resistance to monobromoacetate. The enzyme was purified through (NH4)2SO4 fractionation, DEAE-cellulose chromatography, and hydroxylapatite chromatography. The molecular mass of the protein was 28 kDa as determined with sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 36 kDa as determined with gel filtration on Superose 12 fast protein liquid chromatography. The enzyme was active with 2-halogenated carboxylic acids and converted only the L-isomer of 2-chloropropionic acid with inversion of configuration to produce D-lactate. The activity of the enzyme was not readily influenced by thiol reagents. The gene encoding the haloacid dehalogenase (dhlB) was cloned and could be allocated to a 6.5-kb EcoRI-BglII fragment. Part of this fragment was sequenced, and the dhlB open reading frame was identified by comparison with the N-terminal amino acid sequence of the protein. The gene was found to encode a protein of 27,433 Da that showed considerable homology (60.5 and 61.0% similarity) with the two other haloacid dehalogenases sequenced to date but not with the haloalkane dehalogenase from X. autotrophicus GJ10.

  1,2-二氯乙烷利用细菌黄杆菌自养GJ10的卤酸脱卤酶从表达该酶的突变体中纯化。该突变体是通过选择对单溴乙酸盐具有增强抗性获得的。该酶通过（NH4）2SO4分级、DEAE-纤维素柱层析和羟基磷灰石柱层析纯化。蛋白质的分子量经由SDS-PAGE测定为28 kDa，而超级12快速蛋白液相色谱测定为36 kDa。该酶活性对2-卤代羧酸具有活性，仅转化2-氯丙酸的L异构体，并反向构型生成D-乳酸。该酶的活性不易受到巯基试剂的影响。编码卤酸脱卤酶（dhlB）的基因已被克隆，可分配到一个6.5 kb的EcoRI-BglII片段。该片段的一部分已被序列化，通过与蛋白质N-末端氨基酸序列的比较鉴定了dhlB开放阅读框。发现该基因编码一个蛋白质，分子量为27,433 Da，与迄今为止测序的另外两个卤酸脱卤酶具有相当的同源性（60.5％和61.0％），但与黄杆菌自养GJ10的卤代烷脱卤酶不同。
• 2-Haloacid Dehalogenase from a 4-Chlorobenzoate-Degrading<i>Pseudomonas spec.</i>CBS 3
  作者：Uwe KLAGES、Susanne KRAUSS、Franz LINGENS

  DOI：10.1515/bchm2.1983.364.1.529

  日期：1983.1

  Pseudomonas spec. CBS 3 contains a 2-haloacid dehalogenase induced by chloroacetate. The enzyme was purified about 25-fold to electrophoretic homogeneity by ammonium sulfate fractionation, hydroxyapatite, DEAE-cellulose and gel filtration. The relative molecular masses, as determined by Sephadex G-75 gel filtration and dodecyl sulfate polyacrylamide gel electrophoresis, were 41 000 and 28 000, respectively. The enzyme dehalogenated all monohaloacetates except fluoroacetate. Low activities were found against dichloroacetate and 2,2-dichloropropionate. The enzyme was inactive against trichloroacetate and 3-chloropropionate, it catalysed the stereospecific dehalogenation of L-2-chloropropionate to D-lactate, the rate of dehalogenation being about 20% of the rate of chloroacetate dechlorination. The enzyme activity was not affected by chelating agents and thiol reagents.