p-chloromandelate

• 分子结构分类: 有机化合物 - 苯类化合物 - 苯和取代衍生物
• 英文名称: p-chloromandelate
• 英文别名: (2R)-2-(4-chlorophenyl)-2-hydroxyacetate
• 化学式: C₈H₆ClO₃
• 分子量: 185.587
• InChiKey: BWSFWXSSALIZAU-SSDOTTSWSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  2.1
• 重原子数：
  12
• 可旋转键数：
  1
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.12
• 拓扑面积：
  60.4
• 氢给体数：
  1
• 氢受体数：
  3

反应信息

• 作为反应物：
  描述：

  p-chloromandelate 在 d-mandelate dehydrogenase (DMdh) 作用下， 生成 2-(4-Chlorophenyl)-2-oxoacetate
  参考文献：
  名称：

  Insight into the role of halogen bond in the activity of d-mandelate dehydrogenase toward halogenated substrates

  摘要：

  Chlorine substitution in mandelate turned its derivatives into less active substrates for n-mandelate dehydrogenase (DMdh). To improve the catalysis of chloro-mandelate, a halogen bond was introduced into the protein-substrate complex by site mutation. The catalytic activity of the resulting mutant A89H toward o-chloromandelate was improved by 5 times. The effect of halogen bond was also observed in the dehydrogenation of m-chloromandelate and p-chloromandelate. Based on these results, a new insight was proposed for the role of halogen bond in enzyme activity, and the introduction of halogen bond was shown as an efficient strategy to optimize the catalytic activity toward halogenated substrates. (C) 2016 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.tetlet.2016.03.001
• 作为产物：
  描述：

  (2R)-2-acetyloxy-2-(4-chlorophenyl)acetate 在 citrate synthase 、 acetyl-CoA synthetase 、 Agrobacterium tumefaciens C₅₈ recombinant Atu₃₂₆₆ protein 、 L-malate dehydrogenase 、 β-烟酰胺腺嘌呤二核苷酸 、 水 、 5’-三磷酸腺苷 、 辅酶 A 、 magnesium chloride 作用下， 生成 p-chloromandelate
  参考文献：
  名称：

  Functional Annotation and Three-Dimensional Structure of an Incorrectly Annotated Dihydroorotase from cog3964 in the Amidohydrolase Superfamily

  摘要：

  The substrate specificities of two incorrectly annotated enzymes belonging to cog3964 from the amidohydrolase superfamily were determined. This group of enzymes are currently misannotated as either dihydroorotases or adenine deaminases. Atu3266 from Agrobacterium tumefaciens C58 and Oant2987 from Ochrobactrum anthropi ATCC 49188 were found to catalyze the hydrolysis of acetyl-(R)-mandelate and similar esters with values of K-cat/K-m that exceed 10(5) M-1 s(-1). These enzymes do not catalyze the deamination of adenine or the hydrolysis of dihydroorotate. Atu3266 was crystallized and the structure determined to a resolution of 2.62 angstrom. The protein folds as a distorted (beta/alpha)(8) barrel and binds two zincs in the active site. The substrate profile was determined via a combination of computational docking to the three-dimensional structure of Atu3266 and screening of a highly focused library of potential substrates. The initial weak hit was the hydrolysis of N-acetyl-D-serine (k(cat)/K-m = 4 M-1 s(-1)). This was followed by the progressive identification of acetyl-(R)-glycerate (k(cat)/K-m = 4 x 10(2) M-1 s(-1)), acetyl glycolate (k(cat)/K-m = 1.3 x 10(4) M-1 s(-1)), and ultimately acetyl-(R)-mandelate (k(cat)/K-m = 2.8 x 10(2) M-1 s(-1)).

  DOI：

  10.1021/bi301483z