Lupanine(1+)

• 分子结构分类: 有机化合物 - 生物碱及其衍生物 - 羽扇豆生物碱
• 英文名称: Lupanine(1+)
• 英文别名: (1S,2R,9S,10S)-7-aza-15-azoniatetracyclo[7.7.1.02,7.010,15]heptadecan-6-one
• 化学式: C15H25N2O+
• 分子量: 249.37
• InChiKey: JYIJIIVLEOETIQ-XDQVBPFNSA-O

计算性质

• 辛醇/水分配系数(LogP)：
  1.6
• 重原子数：
  18
• 可旋转键数：
  0
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.93
• 拓扑面积：
  24.8
• 氢给体数：
  1
• 氢受体数：
  1

反应信息

• 作为反应物：
  描述：

  铁阳离子 、 水 、 Lupanine(1+) 生成 17-Hydroxylupanine(1+) 、 铁燧石 、 氢(+1)阳离子
  参考文献：
  名称：

  Lupanine羟化酶，一种降解生物碱的假单胞菌sp。的喹啉细胞色素c。

  摘要：

  Lupanine 17-羟化酶是用于生物碱生物降解的途径中的第一个酶Lupanine，是从假单胞菌属物种中纯化的。酶通过底物的初始脱氢作用，在测定中将细胞色素c用作电子受体。通过超速离心研究的Mr为66,000，通过凝胶过滤的Mr为74,000。可见吸收光谱是细胞色素c的吸收光谱，并且计算出每分子酶分子一个血红素基团的化学计量。SDS / PAGE给出了一个包含haem组的72,000先生带。该酶还含有吡咯并喹啉醌（PQQ），可以通过等电聚焦去除。通过添加PQQ，将辅酶还原为完全活性，并计算出每分子酶中一分子PQQ的化学计量。稳态动力学的值为3。

  DOI：

  10.1042/bj2790105

文献信息

• The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida
  作者：David J. Hopper、Mustak A. Kaderbhai

  DOI：10.1016/s1570-9639(03)00070-0

  日期：2003.4

  Lupanine hydroxylase catalyses the first reaction in the catabolism of the alkaloid lupanine by Pseudomonas putida. It dehydrogenates the substrate, which can then be hydrated. It is a monomeric protein of M, 72,000 and contains a covalently bound haem and a molecule of PQQ. The gene for this enzyme has been cloned and sequenced and the derived protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm. Many of the features seen in the sequence of lupanine hydroxylase are common with other quinoproteins including the W-motifs that are characteristic of the eight-bladed propeller structure of methanol dehydrogenase. However, the unusual disulfide bridge between adjacent cysteines that is present in some PQQ-containing enzymes is absent in lupanine hydroxylase. The C-terminal domain contains characteristics of a cytochrome e and overall the sequence shows similarities with that of the quinohaemoprotein, alcohol dehydrogenase from Comamonas testosteroni. The gene coding for lupanine hydroxylase has been successfully expressed in Escherichia coli and a procedure has been developed to renature and reactivate the enzyme, which was found to be associated with the inclusion bodies. Reactivation required addition of PQQ and was dependent on calcium ions. (C) 2003 Elsevier Science B.V. All rights reserved.