3,4-dihydroxy-2-butanone 4-phosphate | 114155-98-5

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 有机磷酸及其衍生物
• 英文名称: 3,4-dihydroxy-2-butanone 4-phosphate
• 英文别名: 2-Hydroxy-3-oxobutyl phosphate；(2-hydroxy-3-oxobutyl) dihydrogen phosphate
• CAS: 114155-98-5
• 化学式: C₄H₉O₆P
• 分子量: 184.086
• InChiKey: OKYHYXLCTGGOLM-UHFFFAOYSA-N

物化性质

• 沸点：
  425.2±55.0 °C(Predicted)
• 密度：
  1.599±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -2.5
• 重原子数：
  11
• 可旋转键数：
  4
• 环数：
  0.0
• sp3杂化的碳原子比例：
  0.75
• 拓扑面积：
  104
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  [4-¹⁷O_1]-6,7-dimethyl-8-ribityllumazine 、 3,4-dihydroxy-2-butanone 4-phosphate 在 Bacillus subtilis recombinant lumazine synthase 、 Escherichia coli recombinant riboflavin synthase 作用下， 以 aq. buffer 为溶剂， 以95%的产率得到
  参考文献：
  名称：

  Preparation of Flavocoenzyme Isotopologues by Biotransformation of Purines

  摘要：

  Isotope-labeled flavins are crucial reporters for many biophysical studies of flavoproteins. A purine-deficient Escherichia coli strain engineered for expression of the ribAGH genes of Bacillus subtilis converts isotope-labeled purine supplements into the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, with yields up to 40%. The fermentation products can subsequently be converted into isotope-labeled riboflavin and the cognate flavocoenzymes, FMN and FAD, by in vitro biotransformation with better than 90% yield. Using this approach, more than 100 single or multiple C-13-, N-15-, O-17-, and O-18-labeled isotopologues of these cofactors and ligands become easily accessible, enabling advanced ligand-based spectroscopy of flavoproteins and lumazine receptor proteins at unprecedented resolution.

  DOI：

  10.1021/jo502480w
• 作为产物：
  描述：

  (2,3,4-三羟基-5-氧代戊基)磷酸二氢酯 在 Escherichia coli recombinant 3,4-dihydroxybutanone 4-phosphate synthase 、 spinach phosphoriboisomerase 作用下， 以 aq. buffer 为溶剂， 反应 6.0h， 生成 3,4-dihydroxy-2-butanone 4-phosphate
  参考文献：
  名称：

  Preparation of Flavocoenzyme Isotopologues by Biotransformation of Purines

  摘要：

  Isotope-labeled flavins are crucial reporters for many biophysical studies of flavoproteins. A purine-deficient Escherichia coli strain engineered for expression of the ribAGH genes of Bacillus subtilis converts isotope-labeled purine supplements into the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine, with yields up to 40%. The fermentation products can subsequently be converted into isotope-labeled riboflavin and the cognate flavocoenzymes, FMN and FAD, by in vitro biotransformation with better than 90% yield. Using this approach, more than 100 single or multiple C-13-, N-15-, O-17-, and O-18-labeled isotopologues of these cofactors and ligands become easily accessible, enabling advanced ligand-based spectroscopy of flavoproteins and lumazine receptor proteins at unprecedented resolution.

  DOI：

  10.1021/jo502480w

文献信息

• Rate Limitations in the Lumazine Synthase Mechanism
  作者：Ya-Jun Zheng、Paul V. Viitanen、Douglas B. Jordan

  DOI：10.1006/bioo.2000.1163

  日期：2000.4

  7-fold higher than k cat and 20-fold lower than the single-turnover rate. The off rate for the product orthophosphate is about 1 s −1 . Thus, for the M. grisea enzyme at pH 7.5 and 25°C, product dissociation is significantly rate limiting to the steady-state rate of catalysis, whereas the isomerization step limits the single turnover rate. The spinach and E. coli enzymes display a significant lag in pre-steady

  摘要 Lumazine 合酶的催化速度较慢：在 pH 7.5 和 25°C 下，大肠杆菌、稻瘟病菌和菠菜酶的稳态 k cat 值分别为 0.024、0.052 和 0.023 s -1 。在形成连接两个底物 3,4-二羟基-2-丁酮 4-磷酸盐和 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine 的亚胺后，会发生化学上的困难异构化。在 25°C 时，异构化的自由能垒的计算估计值等于或大于 15 kcal/mol。根据 25°C 下大肠杆菌、灰霉病菌和菠菜酶的稳态 k cat 值计算的自由能分别为 19.7、19.2 和 19.7 kcal/mol。M. 在 pH 7.5 和 25°C 下的单次周转率（预稳态）。grisea 酶比稳态速率高 140 倍，它的自由能垒为 16.3 kcal/mol。在稳定前的状态下，M. grisea 酶的 pK a
• Biosynthesis of Riboflavin. Single Turnover Kinetic Analysis of 6,7-Dimethyl-8-ribityllumazine Synthase
  作者：Nicholas Schramek、Ilka Haase、Markus Fischer、Adelbert Bacher

  DOI：10.1021/ja028226k

  日期：2003.4.1

  6,7-dimethyl-8-ribityllumazine synthase (lumazine synthase) catalyzes the condensation of 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione with 3,4-dihydroxy-2-butanone 4-phosphate, affording the riboflavin precursor, 6,7-dimethyl-8-ribityllumazine. Single turnover experiments monitored by multiwavelength photometry were performed with the recombinant lumazine synthase of Bacillus subtilis. Mixing

  6,7-二甲基-8-核嘧啶合酶（lumazine synthase）催化 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione 与 3,4-dihydroxy-2-butanone 4-phosphate 的缩合，提供核黄素前体 6,7-二甲基-8-核黄素。通过多波长光度法监测的单周转实验是用枯草芽孢杆菌的重组 lumazine 合酶进行的。酶与嘧啶类底物的混合有利于低色移以及杂环底物吸光度的降低；该反应的速率常数为 0.02 s(-1) microM(-1)。酶和嘧啶型底物之间的复合物与第二种底物 3,4-二羟基-2-丁酮 4-磷酸快速混合，随后出现早期光学瞬态，其特征是在 330 nm 处的低强度吸收最大值，暂时将其指定为席夫碱中间体。随后磷酸盐的消除提供了在 455 和 282 nm 处具有强烈吸收最大值的瞬态，表明中间体具有扩展的共轭双键系统。随后形成的酶产物
• VOLK, RAINER;BACHER, ADELBERT, J. AMER. CHEM. SOC., 110,(1988) N 11, 3651-3653
  作者：VOLK, RAINER、BACHER, ADELBERT

  DOI：——

  日期：——