(adenylethyl)cobalamine | 59209-78-8

• 分子结构分类: 有机化合物 - 脂质和类脂质分子 - 异戊烯醇脂质
• 英文名称: (adenylethyl)cobalamine
• CAS: 59209-78-8
• 化学式: C₆₉H₉₆CoN₁₈O₁₄P
• 分子量: 1491.6
• InChiKey: YTXPQXKRQKOEQO-WZHZPDAFSA-M

计算性质

• 辛醇/水分配系数(LogP)：
  None
• 重原子数：
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• 可旋转键数：
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• 环数：
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• sp3杂化的碳原子比例：
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• 拓扑面积：
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• 氢给体数：
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• 氢受体数：
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反应信息

• 作为产物：
  描述：

  hydroxocobalamin 、 9-(2-氯-乙基)-9H-嘌呤-6-基胺 在 NaBH₄ 作用下， 以 乙醇 、 水 为溶剂， 生成 (adenylethyl)cobalamine
  参考文献：
  名称：

  X-ray crystallographic and two-dimensional NMR investigations of a coenzyme B12 analog with 5'-deoxyadenosine replaced by 9-(CH2)3-adenine

  摘要：

  The structure of (adeninylpropyl)cobalamin (AdePrCbl), a coenzyme B12 ((5'-deoxyadenosyl)cobalamin) analogue in which the ribose moiety of the adenosyl group has been replaced by a propylene chain, has been determined by X-ray diffraction methods. AdePrCbl crystallizes in the orthorhombic space group P2(1)2(1)2(1), with Z = 4, a = 23.868 (9) angstrom, b = 21.027 (7) angstrom, c = 16.047 (4) angstrom, and v = 8053.07 angstrom3. The final R value is 0.100 based on 6621 observed reflections. The general conformations of the corrin ring, benzimidazole, phosphate, and ribose in AdePrCbl are very similar to those of (5'-deoxyadenosyl)cobalamin and methylcobalamin except for the amide side chains, which show some variability in the oriantations of their amide groups. The adenine ring in AdePrCbl lies over the D ring of the corrin system, rotated about 120-degrees clockwise from its position in coenzyme B-12. The ten water molecules in the crystal structure of AdePrCbl are well located and show no evidence of disorder. Complete H-1 and C-13 NMR assignments of AdePrCbl have been made by using the following two-dimensional NMR methods: homonuclear Hartmann-Hahn spectroscopy (HOHAHA), rotating frame Overhauser enhancement spectroscopy (ROESY), H-1-detected heteronuclear multiple-quantum-coherence (HMQC) spectroscopy, and H-1-detected multiple-bond heteronuclear multiple-quantum-coherence spectroscopy (HMBC). In addition to the adenine orientation found in the crystal structure, a second orientation, in which the adenine lies over the B ring of the corrin, is suggested by H-1 NOEs and by a comparison of the H-1 and C-13 shifts AdePrCbl to those of coenzyme B-12. Our results suggest that alkyladenine groups in cobalamins may have a highly fluxional character permitting several orientations of the adenine. Previous studies have shown that binding to the B-12-dependent enzymes ribonucleotide reductase and diol dehydrase is tighter for (adeninylpentyl)cobalamin than for coenzyme B-12 and the other (adeninylalkyl)cobalamins. On the basis of our studies, we conclude that the flexibility of the alkyl chain, exhibit by the fluxional character of the alkyladenine group, and the orientation of the adenine ring could be responsible for the increased affinity of this analogue for the enzyme. Difference in the orientation of the adenine and the fluxional character of the alkyladenine group, in addition to corrin ring flexibility, may also be useful in explaining the changes in the circular dichroism spectra of (adeninylalkyl)cobalamins upon binding to ethanolamine ammonia-lyase.

  DOI：

  10.1021/ja00002a022