(2R)-sodium 3-phenyllactate | 85391-15-7

• 分子结构分类: 有机化合物 - 苯丙烷和聚酮 - 苯丙酸
• 英文名称: (2R)-sodium 3-phenyllactate
• 英文别名: sodium (2R)-3-phenyllactate；sodium phenyllactate；(R)-2-hydroxy-3-phenyl-propionic acid ; sodium-salt；(R)-2-Hydroxy-3-phenyl-propionsaeure; Natrium-Salz；Sodium (R)-3-phenyllactate；sodium;(2R)-2-hydroxy-3-phenylpropanoate
• CAS: 85391-15-7
• 化学式: C₉H₉O₃*Na
• 分子量: 188.158
• InChiKey: DVSAFLNBVQKEKE-DDWIOCJRSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  -3.66
• 重原子数：
  13
• 可旋转键数：
  3
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.22
• 拓扑面积：
  60.4
• 氢给体数：
  1
• 氢受体数：
  3

安全信息

• 海关编码：
  2918199090

反应信息

• 作为产物：
  描述：

  sodium phenylphyruvate 在 1,4-dihydronicotinamide adenine dinucleotide 、 三羟甲基氨基甲烷盐酸盐 作用下， 以 水 为溶剂， 生成 (2R)-sodium 3-phenyllactate
  参考文献：
  名称：

  A New Family ofD-2-Hydroxyacid Dehydrogenases That ComprisesD-Mandelate Dehydrogenases and 2-Ketopantoate Reductases

  摘要：

  通过活性染色程序和PCR分离粪肠球菌IAM10071的d-扁桃酸脱氢酶(d-ManDH)基因，并在大肠杆菌细胞中表达。该重组酶对各种具有大量疏水侧链的2-酮酸底物，特别是C3支链底物，如苯甲酰甲酸和2-酮异戊酸，表现出高催化活性，并对NADH和NAD+表现出严格的辅酶特异性。它与已知的 NADP 依赖性 2-酮泛解酸还原酶 (KPR) 显示出显着的序列相似性。这些结果表明，d-ManDH 与 KPR 一起构成了一个新的 d-2-羟基酸脱氢酶家族，其作用于 C3 支链 2-酮酸底物，对辅酶和底物具有各种特异性。

  DOI：

  10.1271/bbb.70827

文献信息

• A New Family of<scp>D</scp>-2-Hydroxyacid Dehydrogenases That Comprises<scp>D</scp>-Mandelate Dehydrogenases and 2-Ketopantoate Reductases
  作者：Yusuke WADA、Saho IWAI、Yusuke TAMURA、Tomonori ANDO、Takeshi SHINODA、Kazuhito ARAI、Hayao TAGUCHI

  DOI：10.1271/bbb.70827

  日期：2008.4.23

  The gene for the d-mandelate dehydrogenase (d-ManDH) of Enterococcus faecalis IAM10071 was isolated by means of an activity staining procedure and PCR and expressed in Escherichia coli cells. The recombinant enzyme exhibited high catalytic activity toward various 2-ketoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-ketoisovalerate, and strict coenzyme specificity for NADH and NAD+. It showed marked sequence similarity with known NADP-dependent 2-ketopantoate reductases (KPR). These results indicate that together with KPR, d-ManDH constitutes a new family of d-2-hydroxyacid dehydrogenases that act on C3-branched 2-ketoacid substrates with various specificities for coenzymes and substrates.

  通过活性染色程序和PCR分离粪肠球菌IAM10071的d-扁桃酸脱氢酶(d-ManDH)基因，并在大肠杆菌细胞中表达。该重组酶对各种具有大量疏水侧链的2-酮酸底物，特别是C3支链底物，如苯甲酰甲酸和2-酮异戊酸，表现出高催化活性，并对NADH和NAD+表现出严格的辅酶特异性。它与已知的 NADP 依赖性 2-酮泛解酸还原酶 (KPR) 显示出显着的序列相似性。这些结果表明，d-ManDH 与 KPR 一起构成了一个新的 d-2-羟基酸脱氢酶家族，其作用于 C3 支链 2-酮酸底物，对辅酶和底物具有各种特异性。
• Discovery and characterization of a thermostable d-lactate dehydrogenase from Lactobacillus jensenii through genome mining
  作者：Chanha Jun、Young Seung Sa、Sol-A Gu、Jeong Chan Joo、Seil Kim、Kyung-Jin Kim、Yong Hwan Kim

  DOI：10.1016/j.procbio.2012.11.013

  日期：2013.1

  The demand on thermostable D-lactate dehydrogenases (D-LDH) has been increased for D-lactic acid production but thermostable D-DLHs with industrially applicable activity were not much explored. To identify a thermostable D-LDH, three D-LDHs from different Lactobacillus jensenii strains were screened by genome mining and then expressed in Escherichia coli. One of the three D-LDHs (D-LDH3) exhibited higher optimal reaction temperature (50 degrees C) than the others. The T-50(10) value of this thermostable D-LDH3 was 48.3 degrees C, much higher than the T-50(10) values of the others (42.7 and 42.9 degrees C) and that of a commercial D-lactate dehydrogenase (41.2 degrees C). The T-m values were 48.6, 45.7 and 55.7 degrees C for the three D-LDHs, respectively. In addition, kinetic parameter (k(cat)/K-m) of D-LDH3 for pyruvate reduction was estimated to be almost 150 times higher than that for lactate oxidation at pH 8.0 and 25 degrees C, implying that D-lactate production from pyruvate is highly favored. These superior thermal and kinetic features would make the D-LDH3 characterized in this study a good candidate for the microbial production of D-lactate at high temperature from glucose if it is genetically introduced to lactate producing microbial. Crown Copyright (c) 2012 Published by Elsevier Ltd. All rights reserved.