N6-(Δ2-isopentenyl)adenosine-5'-O-triphosphate | 57596-78-8

• 分子结构分类: 有机化合物 - 核苷、核苷酸和类似物 - 嘌呤核苷酸
• 英文名称: N6-(Δ2-isopentenyl)adenosine-5'-O-triphosphate
• 英文别名: iPR-5'-triphosphate；N⁶-(3-methyl-but-2-enyl)-O^5'-(tetrahydroxy-[1]triphosphoryl)-adenosine；N(6)-(dimethylallyl)adenosine 5'-triphosphate；[[(2R,3S,4R,5R)-3,4-dihydroxy-5-[6-(3-methylbut-2-enylamino)purin-9-yl]oxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate
• CAS: 57596-78-8
• 化学式: C₁₅H₂₄N₅O₁₃P₃
• 分子量: 575.303
• InChiKey: OPLVZTYVQUWKHB-SDBHATRESA-N

物化性质

• 沸点：
  914.6±75.0 °C(Predicted)
• 密度：
  2.06±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -3.5
• 重原子数：
  36
• 可旋转键数：
  11
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.53
• 拓扑面积：
  265
• 氢给体数：
  7
• 氢受体数：
  17

反应信息

• 作为产物：
  描述：

  3-甲基丁-2-烯基膦酰磷酸氢酯 、 5’-三磷酸腺苷 在 adenylate isopentenyl transferase 作用下， 以 various solvents 为溶剂， 反应 2.0h， 生成 N6-(Δ2-isopentenyl)adenosine-5'-O-triphosphate
  参考文献：
  名称：

  Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.)

  摘要：

  A cDNA encoding adenylate isopentenyltransferase (AIPT) was cloned and sequenced from cones of hop (Humulus lupulus L.) by RT-PCR using oligonucleotide primers based on the conserved sequences of Arabidopsis thaliana AIPT isozymes (AtIPT1, AtIPT3, AtIPT4, AtIPT5, AtIPT6, AtIPT7 and AtIPT8). A full-length cDNA contained a 990-by open reading frame encoding a molecular mass of 36,603 Da protein with 329 amino acids. Further, DNA sequencing of genomic DNA revealed absence of introns in the frame. On Southern blot analysis, a single AIPT gene was detected in H. lupulus, while RT-PCR analyses demonstrated that the gene was equally expressed in almost all tissues in the plant including roots, stems, leaves and cones. The deduced amino acid sequence shares 38-51% identity to those of A. thaliana AtIPTs. A recombinant enzyme expressed in Escherichia coli catalyzed isopentenyl transfer reaction from dimethylallyldiphosphate (DMAPP) to the N-6 amino group of adenosine monophosphate (AMP), adenosine diphosphate (ADP) and adenosine triphosphate (ATP), respectively. In contrast, other nucleotides; guanosine monophosphate (GMP), inosine monophosphate (IMP), cytosine monophosphate (CMP), uridine monophosphate (UMP), were not accepted as a substrate. Interestingly, steady-state kinetic analyses revealed that the isopentenylation of ADP and ATP were more efficient than that of AMP as previously reported for A. thaliana AtIPT4. Finally, H. lupulus AIPT contains the putative ATP/GTP binding motif at the N-terminal as in the case of other known isopentenyltransferases. Site-directed mutagenesis of a conserved Asp62, located right after the ATP/GTP binding motif, with Ala resulted in complete loss of enzyme activity. (C) 2004 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.phytochem.2004.08.006

文献信息

• Molecular cloning, expression, and characterization of adenylate isopentenyltransferase from hop (Humulus lupulus L.)
  作者：Yuichi Sakano、Yukio Okada、Akiko Matsunaga、Takaharu Suwama、Takafumi Kaneko、Kazutoshi Ito、Hiroshi Noguchi、Ikuro Abe

  DOI：10.1016/j.phytochem.2004.08.006

  日期：2004.9

  A cDNA encoding adenylate isopentenyltransferase (AIPT) was cloned and sequenced from cones of hop (Humulus lupulus L.) by RT-PCR using oligonucleotide primers based on the conserved sequences of Arabidopsis thaliana AIPT isozymes (AtIPT1, AtIPT3, AtIPT4, AtIPT5, AtIPT6, AtIPT7 and AtIPT8). A full-length cDNA contained a 990-by open reading frame encoding a molecular mass of 36,603 Da protein with 329 amino acids. Further, DNA sequencing of genomic DNA revealed absence of introns in the frame. On Southern blot analysis, a single AIPT gene was detected in H. lupulus, while RT-PCR analyses demonstrated that the gene was equally expressed in almost all tissues in the plant including roots, stems, leaves and cones. The deduced amino acid sequence shares 38-51% identity to those of A. thaliana AtIPTs. A recombinant enzyme expressed in Escherichia coli catalyzed isopentenyl transfer reaction from dimethylallyldiphosphate (DMAPP) to the N-6 amino group of adenosine monophosphate (AMP), adenosine diphosphate (ADP) and adenosine triphosphate (ATP), respectively. In contrast, other nucleotides; guanosine monophosphate (GMP), inosine monophosphate (IMP), cytosine monophosphate (CMP), uridine monophosphate (UMP), were not accepted as a substrate. Interestingly, steady-state kinetic analyses revealed that the isopentenylation of ADP and ATP were more efficient than that of AMP as previously reported for A. thaliana AtIPT4. Finally, H. lupulus AIPT contains the putative ATP/GTP binding motif at the N-terminal as in the case of other known isopentenyltransferases. Site-directed mutagenesis of a conserved Asp62, located right after the ATP/GTP binding motif, with Ala resulted in complete loss of enzyme activity. (C) 2004 Elsevier Ltd. All rights reserved.