(3S,4aS,5S,6S,7S,11S,12aS)-1,2,3,4,4a,5,6,7,8,11,12,12a-dodecahydro-9,12a,13,13-tetramethyl-4-methylene-6,10-methanobenzocyclodecene-3,5,7,11-tetrol 5-acetate | 849705-68-6

• 英文名称: (3S,4aS,5S,6S,7S,11S,12aS)-1,2,3,4,4a,5,6,7,8,11,12,12a-dodecahydro-9,12a,13,13-tetramethyl-4-methylene-6,10-methanobenzocyclodecene-3,5,7,11-tetrol 5-acetate
• 英文别名: 5α,10β,14β-trihydroxy-2α-acetoxytaxa-4(20),11(12)-diene；5,10,14-desacetyl taxuyunnanine C；(2α,5α,10β,14β)-taxa-4(20),11-diene-2,5,10,14-tetrol 2-acetate；[(1S,2S,3S,5S,8S,10S,14S)-5,10,14-trihydroxy-8,12,15,15-tetramethyl-4-methylidene-2-tricyclo[9.3.1.03,8]pentadec-11-enyl] acetate
• CAS: 849705-68-6
• 化学式: C₂₂H₃₄O₅
• 分子量: 378.509
• InChiKey: HCGFDDIDDXJVGM-YIJNTCITSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  1.4
• 重原子数：
  27
• 可旋转键数：
  2
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.77
• 拓扑面积：
  87
• 氢给体数：
  3
• 氢受体数：
  5

反应信息

• 作为反应物：
  描述：

  乙酰辅酶A 、 (3S,4aS,5S,6S,7S,11S,12aS)-1,2,3,4,4a,5,6,7,8,11,12,12a-dodecahydro-9,12a,13,13-tetramethyl-4-methylene-6,10-methanobenzocyclodecene-3,5,7,11-tetrol 5-acetate 以 二甲基亚砜 为溶剂， 反应 0.5h， 生成 taxuyunnanin C
  参考文献：
  名称：

  Special publicationfn1fn1Papers with this heading have received accelerated publication, due to their particular significance in the field of phytochemistry. Purification and characterization of acetyl coenzyme a: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis

  摘要：

  An O-acetyltransferase that catalyzes the regiospecific acetylation of a range of taxanes possessing an unsubstituted 10-hydroxyl group was detected and purified to apparent electrophoretic homogeneity from a cytosolic fraction of Taxus chinensis cell cultures. The purification involved negative calcium phosphate adsorption, sephadex desalting, DEAE, AcA44 chromatography, HighQ, CHT II, HiTrap Blue, Phenylsepharose and Mimetic Green purification steps. The purified acetyltransferase was found to be a monomeric protein of 71 +/- 1.5 kDa that is highly regio- and stereospecific towards the 10 beta-hydroxyl group of the taxane molecule and is also active towards 10-desacetylbaccatine III. The acetyltransferase reaction had a pH optimum of 9.0 with halfmaximal activities at pH 6.8 and 10.8, respectively. The temperature optimum was at 35 degrees C and the isoelectric point at 5.6. The apparent K-m values for 10-desacetyltaxuyunnanine C and acetyl CoA were 23 and 61 mu M, respectively. The turnover rate for the enzyme using both substrates was 0.2 mol mol(-1) of enzyme. The kinetic optimum was determined to be K-cat/K-m = 8.7 s(-1) L M-1. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0031-9422(98)00674-8
• 作为产物：
  描述：

  taxuyunnanin C 在 sodium hydroxide 作用下， 以 甲醇 为溶剂， 以60%的产率得到10β-hydroxy-2α,5α14β-triacetoxytaxa-4(20),11(12)-diene
  参考文献：
  名称：

  Special publicationfn1fn1Papers with this heading have received accelerated publication, due to their particular significance in the field of phytochemistry. Purification and characterization of acetyl coenzyme a: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis

  摘要：

  An O-acetyltransferase that catalyzes the regiospecific acetylation of a range of taxanes possessing an unsubstituted 10-hydroxyl group was detected and purified to apparent electrophoretic homogeneity from a cytosolic fraction of Taxus chinensis cell cultures. The purification involved negative calcium phosphate adsorption, sephadex desalting, DEAE, AcA44 chromatography, HighQ, CHT II, HiTrap Blue, Phenylsepharose and Mimetic Green purification steps. The purified acetyltransferase was found to be a monomeric protein of 71 +/- 1.5 kDa that is highly regio- and stereospecific towards the 10 beta-hydroxyl group of the taxane molecule and is also active towards 10-desacetylbaccatine III. The acetyltransferase reaction had a pH optimum of 9.0 with halfmaximal activities at pH 6.8 and 10.8, respectively. The temperature optimum was at 35 degrees C and the isoelectric point at 5.6. The apparent K-m values for 10-desacetyltaxuyunnanine C and acetyl CoA were 23 and 61 mu M, respectively. The turnover rate for the enzyme using both substrates was 0.2 mol mol(-1) of enzyme. The kinetic optimum was determined to be K-cat/K-m = 8.7 s(-1) L M-1. (C) 1999 Elsevier Science Ltd. All rights reserved.

  DOI：

  10.1016/s0031-9422(98)00674-8