γ-L-glutamyl-p-nitroanilide

• 分子结构分类: 有机化合物 - 有机酸及其衍生物 - 羧酸及其衍生物
• 英文名称: γ-L-glutamyl-p-nitroanilide
• 英文别名: L-γ-glutamyl-p-nitroanilide；gamma-glutamyl-p-nitroanilide；glutamyl p-nitroanilide；GPNA；2-azaniumyl-5-(4-nitroanilino)-5-oxopentanoate
• 化学式: C₁₁H₁₃N₃O₅
• 分子量: 267.241
• InChiKey: WMZTYIRRBCGARG-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -2.4
• 重原子数：
  19
• 可旋转键数：
  5
• 环数：
  1.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  138
• 氢给体数：
  3
• 氢受体数：
  6

反应信息

• 作为反应物：
  描述：

  γ-L-glutamyl-p-nitroanilide 在 recombinant At₄g30530 (GGP₁) 作用下， 生成 4-硝基苯胺
  参考文献：
  名称：

  Biosynthetic engineering of glucosinolates

  摘要：

  这项发明提供了一种将宿主从无法进行糖苷硫酸盐（GSL）生物合成或从氨基酸GSL前体进行链延长的表型转变为能够进行该生物合成或延长的表型的方法和材料，例如新鉴定的基因和新颖的过程。

  公开号：

  US09096863B2

文献信息

• Biosynthetic engineering of glucosinolates
  申请人：Geu Flores Fernando

  公开号：US09096863B2

  公开（公告）日：2015-08-04

  The invention provides methods and materials, such as newly characterized genes, and novel processes, for converting a host from a phenotype whereby the host is unable to carry out glucosinolate (GSL) biosynthesis or chain elongation from an amino acid GSL-precursor to a phenotype whereby the host carries out said biosynthesis or elongation.

  这项发明提供了一种将宿主从无法进行糖苷硫酸盐（GSL）生物合成或从氨基酸GSL前体进行链延长的表型转变为能够进行该生物合成或延长的表型的方法和材料，例如新鉴定的基因和新颖的过程。
• γ-Glutamyl transpeptidase architecture: Effect of extra sequence deletion on autoprocessing, structure and stability of the protein from Bacillus licheniformis
  作者：Meng-Chun Chi、Yi-Hui Lo、Yi-Yu Chen、Long-Liu Lin、Antonello Merlino

  DOI：10.1016/j.bbapap.2014.09.001

  日期：2014.12

  gamma-Glutamyl transpeptidases (gamma-GTs, EC 23.2.2) are a class of ubiquitous enzymes which initiate the cleavage of extracellular glutathione (gamma-Glu-Cys-Gly, GSH) into its constituent glutamate, cysteine, and glycine and catalyze the transfer of its gamma-glutamyl group to water (hydrolysis), amino acids or small peptides (transpeptidation). These proteins utilize a conserved Thr residue to process their chains into a large and a small subunit that then form the catalytically competent enzyme. Multiple sequence alignments have shown that some bacterial gamma-GTs, including that from Bacillus licheniformis (BlGT), possess an extra sequence at the C-terminal tail of the large subunit, whose role is unknown. Here, autoprocessing, structure, catalytic activity and stability against both temperature and the chemical denaturant guanidinium hydrochloride of six BlGT extra-sequence deletion mutants have been characterized by SDS-PAGE, circular dichroism, intrinsic fluorescence and homology modeling. Data suggest that the extra sequence has a crucial role in enzyme activation and structural stability. Our results assist in the development of a structure-based interpretation of the autoprocessing reaction of gamma-GTs and are helpful to unveil the molecular bases of their structural stability. (C) 2014 Elsevier B.V. All rights reserved.