5,10-methenyltetrahydromethanopterin | 89455-79-8

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物
• 英文名称: 5,10-methenyltetrahydromethanopterin
• 英文别名: methenyltetrahydromethanoptherin；methenyl-H4MPT+；Carboxy-5,6,7,8-tetrahydromethanopterin；[(2R,3S,4R,5S)-5-[(2R,3S,4S)-5-[4-[(6S,6aR,7R)-3-amino-6,7-dimethyl-1-oxo-5,6,6a,7-tetrahydro-2H-imidazo[1,5-f]pteridin-10-ium-8-yl]phenyl]-2,3,4-trihydroxypentoxy]-3,4-dihydroxyoxolan-2-yl]methyl [(1S)-1,3-dicarboxypropyl] phosphate
• CAS: 89455-79-8
• 化学式: C₃₁H₄₃N₆O₁₆P
• 分子量: 786.687
• InChiKey: RANKJVUGLXUXOL-CAFBYHECSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  -4.6
• 重原子数：
  54
• 可旋转键数：
  17
• 环数：
  5.0
• sp3杂化的碳原子比例：
  0.58
• 拓扑面积：
  339
• 氢给体数：
  10
• 氢受体数：
  17

反应信息

• 作为反应物：
  描述：

  5,10-methenyltetrahydromethanopterin 在 5,10-methenyltetrahydromethanopterin hydrogenase II from Methanocaldococcus jannaschii holo type 、 氢气 作用下， 以 aq. phosphate buffer 为溶剂， 生成 5,10-methylenetetrahydromethanopterin
  参考文献：
  名称：

  Towards a functional identification of catalytically inactive [Fe]‐hydrogenase paralogs

  摘要：

  [Fe]‐hydrogenase (Hmd), an enzyme of the methanogenic energy metabolism, harbors an iron‐guanylylpyridinol (FeGP) cofactor used for H2 cleavage. The generated hydride is transferred to methenyl‐tetrahydromethanopterin (methenyl‐H4MPT+). Most hydrogenotrophic methanogens contain the hmd‐related genes hmdII and hmdIII. Their function is still elusive. We were able to reconstitute the HmdII holoenzyme of Methanocaldococcus jannaschii with recombinantly produced apoenzyme and the FeGP cofactor, which is a prerequisite for in vitro functional analysis. Infrared spectroscopic and X‐ray structural data clearly indicated binding of the FeGP cofactor. Methylene‐H4MPT binding was detectable in the significantly altered infrared spectra of the HmdII holoenzyme and in the HmdII apoenzyme–methylene‐H4MPT complex structure. The related binding mode of the FeGP cofactor and methenyl‐H4MPT+ compared with Hmd and their multiple contacts to the polypeptide highly suggest a biological role in HmdII. However, holo‐HmdII did not catalyze the Hmd reaction, not even in a single turnover process, as demonstrated by kinetic measurements. The found inactivity can be rationalized by an increased contact area between the C‐ and N‐terminal folding units in HmdII compared with in Hmd, which impairs the catalytically necessary open‐to‐close transition, and by an exchange of a crucial histidine to a tyrosine. Mainly based on the presented data, a function of HmdII as Hmd isoenzyme, H2 sensor, FeGP‐cofactor storage protein and scaffold protein for FeGP‐cofactor biosynthesis could be excluded. Inspired by the recently found binding of HmdII to aminoacyl‐tRNA synthetases and tRNA, we tentatively consider HmdII as a regulatory protein for protein synthesis that senses the intracellular methylene‐H4MPT concentration.DatabaseStructural data are available in the Protein Data Bank under the accession numbers 4YT8; 4YT2; 4YT4 and 4YT5.

  DOI：

  10.1111/febs.13351
• 作为产物：
  描述：

  5,10-methylenetetrahydromethanopterin 在 Methanobrevibacter smithii cell extract 作用下， 生成 5,10-methenyltetrahydromethanopterin
  参考文献：
  名称：

  通过稳定同位素标记阐明的产甲烷古细菌中 [Fe]-氢化酶的铁-鸟苷酰吡啶醇辅因子的生物合成

  摘要：

  [Fe]-氢化酶催化从 H(2) 到methenyltetrahydromethanopherin 的可逆氢化物转移，它是产甲烷古细菌中从H(2) 和CO(2) 形成甲烷的中间体。该酶具有独特的活性位点铁-鸟苷基吡啶醇 (FeGP) 辅因子，其中低自旋 Fe(II) 由吡啶醇-N、酰基、两个一氧化碳和酶的半胱氨酸的硫配位。在这里，我们通过将来自标记前体的 (13)C 和 (2)H 掺入到生长产甲烷古菌的辅因子中，并通过随后的 NMR、基质辅助激光解吸/电离时间来研究 FeGP 辅因子的生物合成。飞行质谱（MALDI-TOF-MS），电喷雾电离傅立叶变换离子回旋共振质谱 (ESI-FT-ICR-MS) 和 IR 分析分离的辅因子和参考化合物。发现辅因子的吡啶醇部分由三个乙酸的 C-1、两个乙酸的 C-2、两个丙酮酸的 C-1、一个来自 l-甲硫氨酸的甲基的碳和一个直接来自 CO的碳合成(2)

  DOI：

  10.1021/ja211594m