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2,4-dinitrophenyl 1,4-β-D-galactobioside | 200504-60-5

中文名称
——
中文别名
——
英文名称
2,4-dinitrophenyl 1,4-β-D-galactobioside
英文别名
——
2,4-dinitrophenyl 1,4-β-D-galactobioside化学式
CAS
200504-60-5
化学式
C18H24N2O15
mdl
——
分子量
508.393
InChiKey
AQJZDRFAWVURAR-BQVHMPCVSA-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

反应信息

  • 作为反应物:
    参考文献:
    名称:
    Activity of three β-1,4-galactanases on small chromogenic substrates
    摘要:
    beta-1,4-Galactanases belong to glycoside hydrolase family GH 53 and degrade galactan and arabinogalactan side chains of the complex pectin network in plant cell walls. Two fungal beta-1,4-galactanases from Aspergillus aculeatus, Meripileus giganteus and one bacterial enzyme from Bacillus licheniformis have been kinetically characterized using the chromogenic substrate analog 4-nitrophenyl beta-1,4-D-thiogalactobioside synthesized by the thioglycoligase approach. Values of k(cat)/K-m for this substrate with A. aculeatus beta-1,4-galactanase at pH 4.4 and for M. giganteus beta-1,4-galactanase at pH 5.5 are 333 M (1) s (1) and 62 M (1) s (1), respectively. By contrast the B. licheniformis beta-1,4-galactanase did not hydrolyze 4-nitrophenyl beta-1,4-D-thiogalactobioside. The different kinetic behavior observed between the two fungal and the bacterial beta-1,4-galactanases can be ascribed to an especially long loop 8 observed only in the structure of B. licheniformis beta-1,4-galactanase. This loop contains substrate binding subsites -3 and -4, which presumably cause B. licheniformis beta-1,4-galactanase to bind 4-nitrophenyl -1,4-beta-D-thiogalactobioside non-productively. In addition to their cleavage of 4-nitrophenyl -1,4-beta-D-thiogalactobioside, the two fungal enzymes also cleaved the commercially available 2-nitrophenyl-1,4-beta-D-galactopyranoside, but kinetic parameters could not be determined because of transglycosylation at substrate concentrations above 4 mM. (C) 2011 Elsevier Ltd. All rights reserved.
    DOI:
    10.1016/j.carres.2011.05.017
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