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factor III octamethyl ester

中文名称
——
中文别名
——
英文名称
factor III octamethyl ester
英文别名
——
factor III octamethyl ester化学式
CAS
——
化学式
C51H64N4O16
mdl
——
分子量
989.086
InChiKey
IEDYMUJKPHVARA-GUCGZNTNSA-N
BEILSTEIN
——
EINECS
——
  • 物化性质
  • 计算性质
  • ADMET
  • 安全信息
  • SDS
  • 制备方法与用途
  • 上下游信息
  • 反应信息
  • 文献信息
  • 表征谱图
  • 同类化合物
  • 相关功能分类
  • 相关结构分类

计算性质

  • 辛醇/水分配系数(LogP):
    5.71
  • 重原子数:
    71.0
  • 可旋转键数:
    20.0
  • 环数:
    5.0
  • sp3杂化的碳原子比例:
    0.53
  • 拓扑面积:
    267.76
  • 氢给体数:
    2.0
  • 氢受体数:
    18.0

反应信息

  • 作为产物:
    描述:
    甲醇S-腺苷-L-蛋氨酸尿紫元(III) 在 antifoam 204 、 magnesium chloride Tris-HCl buffer 、 Escherichia coli CR395 lysate 、 potassium chloride 、 硫酸 作用下, 反应 38.0h, 以6%的产率得到
    参考文献:
    名称:
    Synthesis of substrate analogs of methyltransferases in the vitamin B12 biosynthetic pathway and characterization of their enzymatic products
    摘要:
    The specificity toward substrate analogs of the first two methyltransferases in the vitamin B-12 biosynthetic pathway was probed with 15 synthetic porphyrinogens. Several novel methylated chlorins and isobacteriochlorins were isolated and characterized, suggesting the same methylation sequence C-2 > C-7 > C-20 as for the natural substrate, uro'gen III. The results allow us to narrow down possible structural requirements concerning substrate recognition by the methyltransferase enzymes. (c) 2006 Elsevier Ltd. All rights reserved.
    DOI:
    10.1016/j.bmc.2006.01.041
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文献信息

  • Synthesis of substrate analogs of methyltransferases in the vitamin B12 biosynthetic pathway and characterization of their enzymatic products
    作者:Clotilde Pichon-Santander、Patricio J. Santander、A. Ian Scott
    DOI:10.1016/j.bmc.2006.01.041
    日期:2006.6
    The specificity toward substrate analogs of the first two methyltransferases in the vitamin B-12 biosynthetic pathway was probed with 15 synthetic porphyrinogens. Several novel methylated chlorins and isobacteriochlorins were isolated and characterized, suggesting the same methylation sequence C-2 > C-7 > C-20 as for the natural substrate, uro'gen III. The results allow us to narrow down possible structural requirements concerning substrate recognition by the methyltransferase enzymes. (c) 2006 Elsevier Ltd. All rights reserved.
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