Guanosin-5'-monophosphorsaeure, 32P-markiert | 36792-14-0

• 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: Guanosin-5'-monophosphorsaeure, 32P-markiert
• 英文别名: 5'-[32P]-G；[³²P][5']guanylic acid
• CAS: 36792-14-0
• 化学式: C₁₀H₁₄N₅O₈P
• 分子量: 364.25
• InChiKey: RQFCJASXJCIDSX-BDNGZQIKSA-N

反应信息

• 作为反应物：
  描述：

  Guanosin-5'-monophosphorsaeure, 32P-markiert 在 piruvate kinase 、 T₅ bacteriophage deoxynucleoside monophosphate kinase 作用下， 生成 [α-(32)P]GTP
  参考文献：
  名称：

  T5噬菌体脱氧核糖核苷单磷酸激酶的底物特异性及其在[α-32P]d/rNTP合成中的应用

  摘要：

  噬菌体 T5 脱氧核苷单磷酸激酶（dNMP 激酶，EC 2.7.4.13）显示可催化 d2CMP 和核糖核苷酸 AMP、GMP 和 CMP 的磷酸化，但不磷酸化 UMP。对于磷酰基的天然受体，发现了 km 和 kcat。T5 dNMP 激酶作为能够磷酸化标记的 r/dNMP 的通用酶的适用性已被证明可用于合成 [α-32P]rNTP 和 [α-32P]dNTP。

  DOI：

  10.1134/s1068162009060090
• 作为产物：
  描述：

  5'-[32P]-GGG 在 recombinant human poly(A)-specific ribonuclease 、 sodium chloride 、 magnesium chloride 、 bovine serum albumin 作用下， 反应 0.17h， 生成 Guanosin-5'-monophosphorsaeure, 32P-markiert 、 5'-[32P]-GG
  参考文献：
  名称：

  Recognition of Adenosine Residues by the Active Site of Poly(A)-specific Ribonuclease

  摘要：

  Poly(A)-specific ribonuclease (PARN) is a mammalian 3'-exoribonuclease that degrades poly(A) with high specificity. To reveal mechanisms by which poly(A) is recognized by the active site of PARN, we have performed a kinetic analysis using a large repertoire of trinucleotide substrates. Our analysis demonstrated that PARN harbors specificity for adenosine recognition in its active site and that the nucleotides surrounding the scissile bond are critical for adenosine recognition. We propose that two binding pockets, which interact with the nucleotides surrounding the scissile bond, play a pivotal role in providing specificity for the recognition of adenosine residues by the active site of PARN. In addition, we show that PARN, besides poly(A), also quite efficiently degrades poly(U), similar to 10-fold less efficiently than poly(A). The poly(U)-degrading property of PARN could be of biological significance as oligo(U) tails recently have been proposed to play a role in RNA stabilization and destabilization.

  DOI：

  10.1074/jbc.m109.043893