5'-Deoxyadenosine
(Synonyms: 5-脱氧腺嘌呤核苷) 目录号 : GC33636
An adenosine analog
Cas No.:4754-39-6
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
5’-Deoxyadenosine is an analog of adenosine and an intermediate in the degradation of S-adenosylmethionine (SAM).1 It has been used in the study of enzyme kinetics, including those of phosphomethylpyrimidine synthase, glutamate mutase, and 5’-methylthioadenosine phosphorylase.2,3,4
1.Grove, T.L., Lee, K.-H., St. Clair, J., et al.In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clustersBiochemistry47(28)7523-7538(2008) 2.Palmer, L.D., and Downs, D.M.The thiamine biosynthetic enzyme ThiC catalyzes multiple turnovers and is inhibited by S-adenosylmethionine (AdoMet) metabolitesJ. Biol. Chem.288(42)30693-30699(2013) 3.Chen, H.P., and Marsh, E.N.Adenosylcobalamin-dependent glutamate mutase: Examination of substrate and coenzyme binding in an engineered fusion protein possessing simplified subunit structure and kinetic propertiesBiochemistry36(48)14939-14945(1997) 4.Savarese, T.M., Crabtree, G.W., and Parks, J., R.E.5'-Methylthioadenosine phosphorylase-I substrate activity of 5'-deoxyadenosine with the enzyme from sarcoma 180 cellsBiochem. Pharmacol.30(3)189-199(1981)
| Cas No. | 4754-39-6 | SDF | |
| 别名 | 5-脱氧腺嘌呤核苷 | ||
| Canonical SMILES | C[C@@H]1[C@H]([C@H]([C@H](N2C=NC3=C2N=CN=C3N)O1)O)O | ||
| 分子式 | C10H13N5O3 | 分子量 | 251.24 |
| 溶解度 | DMSO : 125 mg/mL (497.53 mM) | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 3.9803 mL | 19.9013 mL | 39.8026 mL |
| 5 mM | 0.7961 mL | 3.9803 mL | 7.9605 mL |
| 10 mM | 0.398 mL | 1.9901 mL | 3.9803 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Transition State Analogue Inhibitors of 5'-Deoxyadenosine/5'-Methylthioadenosine Nucleosidase from Mycobacterium tuberculosis
Biochemistry 2017 Sep 26;56(38):5090-5098.PMID:28836767DOI:10.1021/acs.biochem.7b00576.
Mycobacterium tuberculosis 5'-Deoxyadenosine/5'-methylthioadenosine nucleosidase (Rv0091) catalyzes the N-riboside hydrolysis of its substrates 5'-methylthioadenosine (MTA) and 5'-Deoxyadenosine (5'-dAdo). 5'-dAdo is the preferred substrate, a product of radical S-adenosylmethionine-dependent enzyme reactions. Rv0091 is characterized by a ribocation-like transition state, with low N-ribosidic bond order, an N7-protonated adenine leaving group, and an activated but weakly bonded water nucleophile. DADMe-Immucillins incorporating 5'-substituents of the substrates 5'-dAdo and MTA were synthesized and characterized as inhibitors of Rv0091. 5'-Deoxy-DADMe-Immucillin-A was the most potent among the 5'-dAdo transition state analogues with a dissociation constant of 640 pM. Among the 5'-thio substituents, hexylthio-DADMe-Immucillin-A was the best inhibitor at 87 pM. The specificity of Rv0091 for the Immucillin transition state analogues differs from those of other bacterial homologues because of an altered hydrophobic tunnel accepting the 5'-substituents. Inhibitors of Rv0091 had weak cell growth effects on M. tuberculosis or Mycobacterium smegmatis but were lethal toward Helicobacter pylori, where the 5'-methylthioadenosine nucleosidase is essential in menaquinone biosynthesis. We propose that Rv0091 plays a role in 5'-Deoxyadenosine recycling but is not essential for growth in these Mycobacteria.
The B12-independent glycerol dehydratase activating enzyme from Clostridium butyricum cleaves SAM to produce 5'-Deoxyadenosine and not 5'-deoxy-5'-(methylthio)adenosine
J Inorg Biochem 2022 Feb;227:111662.PMID:34847521DOI:10.1016/j.jinorgbio.2021.111662.
Glycerol dehydratase activating enzyme (GD-AE) is a radical S-adenosyl-l-methionine (SAM) enzyme that installs a catalytically essential amino acid backbone radical onto glycerol dehydratase in bacteria under anaerobic conditions. Although GD-AE is closely homologous to other radical SAM activases that have been shown to cleave the S-C(5') bond of SAM to produce 5'-Deoxyadenosine (5'-dAdoH) and methionine, GD-AE from Clostridium butyricum has been reported to instead cleave the S-C(γ) bond of SAM to yield 5'-deoxy-5'-(methylthio)adenosine (MTA). Here we re-investigate the SAM cleavage reaction catalyzed by GD-AE and show that it produces the widely observed 5'-dAdoH, and not the less conventional product MTA.
Travels with carbon-centered radicals. 5'-Deoxyadenosine and 5'-deoxyadenosine-5'-yl in radical enzymology
Acc Chem Res 2014 Feb 18;47(2):540-9.PMID:24308628DOI:10.1021/ar400194k.
As a graduate student under Professor R. H. Abeles, I began my journey with 5'-Deoxyadenosine, studying the coenzyme B12 (adenosylcobalamin)-dependent dioldehydrase (DDH). I proved that suicide inactivation of dioldehydrase by glycolaldehyde proceeded with irreversible cleavage of adenosylcobalamin to 5'-Deoxyadenosine. I further showed that suicide inactivation by [2-(3)H]glycolaldehyde produced 5'-deoxy[(3)H]adenosine, the first demonstration of hydrogen transfer to adenosyl-C5' of adenosylcobalamin. The tritium kinetic isotope effect (T)k was 15, which correlated well with the measurement (D)k = 12 for transformation of [1-(2)H]propane-1,2-diol to [2-(2)H]propionaldehyde by DDH. After establishing my own research program, I returned to the glycolaldehyde inactivation of DDH, showing by EPR that suicide inactivation produced glycolaldehyde-2-yl. In retrospect, suicide inactivation involved scission of adenosylcobalamin to 5'-deoxyadenosine-5'-yl, which abstracted a hydrogen from glycolaldehyde. Captodative-stabilized glycolaldehyde-2-yl could not react further, leading to suicide inactivation. In 1986, my colleagues and I took up the problem of the mechanism by which lysine 2,3-aminomutase (LAM) catalyzes S-adenosylmethionine (SAM) and pyridoxal-5'-phosphate (PLP)-dependent interconversion of l-lysine and l-β-lysine. Because the reaction followed the pattern of adenosylcobalamin-dependent rearrangements, I postulated that SAM might be an evolutionary predecessor to adenosylcobalamin. Testing this hypothesis, we traced hydrogen transfer from lysine through the adenosyl-C5' of SAM to β-lysine. Thus, the 5'-deoxyadenosyl of SAM mediated hydrogen transfer by LAM exactly as in adenosylcobalamin mediated hydrogen transfer in B12-dependent isomerizations. The mechanism postulated that SAM cleaves to form 5'-deoxyadenosine-5'-yl followed by abstraction of C3(H) from PLP-α-lysine aldimine to form PLP-α-lysine-3-yl. PLP-α-lysine-3-yl isomerizes to pyridoxal-β-lysine-2-yl, and a hydrogen abstraction from 5'-Deoxyadenosine regenerates 5'-deoxyadenosine-5'-yl and releases β-lysine. Of four radicals in the postulated mechanism, three have been characterized by EPR spectroscopy as kinetically competent intermediates. The analysis of the role of iron allowed researchers to elucidate the mechanism by which SAM is cleaved to 5'-deoxyadenosine-5'-yl. LAM contains one [4Fe-4S] cluster ligated by three cysteine residues. As shown by ENDOR spectroscopy and X-ray crystallography, the fourth ligand to the cluster is SAM, through the methionyl carboxylate and amino groups. Inner sphere electron transfer within the [4Fe-4S](1+)-SAM complex leads to [4Fe-4S](2+)-Met and 5'-deoxyadenosine-5'-yl. The iron-binding motif in LAM, CxxxCxxC, found by other groups in four other SAM-dependent enzymes, is the founding motif for the radical SAM superfamily. These enzymes number in the tens of thousands and are responsible for highly diverse and chemically difficult transformations in the biosphere. Available information supports the hypothesis that this superfamily provides the chemical context from which the much more structurally complex adenosylcobalamin evolved.
5'-Deoxyadenosine metabolism in various mammalian cell lines
Biochem Pharmacol 1983 Apr 15;32(8):1433-40.PMID:6602613DOI:10.1016/0006-2952(83)90458-6.
5'-Deoxyadenosine (5'-dAdo) was rapidly cleaved to adenine by cell-free, dialyzed extracts of Chinese hamster ovary (CHO), Novikoff rat hepatoma and HeLa cells in a phosphate-dependent reaction, but not by extracts from L929, L1210 and P388 cells. Radioactivity from [5'-3H]5'-dAdo was incorporated into the acid-soluble pool (uptake) by whole CHO, Novikoff and HeLa cells almost as rapidly as from labeled adenosine or adenine (all at 5 microM extracellular concentration). Radioactivity in the acid-soluble pool was mainly associated with a component identified as 5-deoxyribose-1-phosphate. Compared to ribose-1-phosphate, 5-deoxyribose-1-phosphate was metabolically highly stable. A second labeled component, however, was formed slowly and accumulated mainly in the medium. Its formation was greatly stimulated by hypoxanthine and, under conditions where their deamination was not blocked, by adenosine and 2'- and 3'-deoxyadenosine. The second product was 5'-deoxyinosine synthesized from hypoxanthine and 5-deoxyribose-1-phosphate by purine nucleoside phosphorylase. Cleavage of 5'-dAdo by whole cells was dependent on the continuous removal of the product adenine, since uptake was greatly reduced in cells deficient in adenine phosphoribosyl transferase and 50 microM adenine strongly inhibited 5'-dAdo cleavage. The results are consistent with the view that 5'-dAdo is a substrate for 5'-methylthioadenosine phosphorylase and that its use as a non-metabolizable substrate for the nucleoside transport measurements is limited to cells lacking this enzyme.
Identification of a 5'-Deoxyadenosine deaminase in Methanocaldococcus jannaschii and its possible role in recycling the radical S-adenosylmethionine enzyme reaction product 5'-Deoxyadenosine
J Bacteriol 2014 Mar;196(5):1064-72.PMID:24375099DOI:10.1128/JB.01308-13.
We characterize here the MJ1541 gene product from Methanocaldococcus jannaschii, an enzyme that was annotated as a 5'-methylthioadenosine/S-adenosylhomocysteine deaminase (EC 3.5.4.31/3.5.4.28). The MJ1541 gene product catalyzes the conversion of 5'-Deoxyadenosine to 5'-deoxyinosine as its major product but will also deaminate 5'-methylthioadenosine, S-adenosylhomocysteine, and adenosine to a small extent. On the basis of these findings, we are naming this new enzyme 5'-Deoxyadenosine deaminase (DadD). The Km for 5'-Deoxyadenosine was found to be 14.0 ± 1.2 μM with a kcat/Km of 9.1 × 10(9) M(-1) s(-1). Radical S-adenosylmethionine (SAM) enzymes account for nearly 2% of the M. jannaschii genome, where the major SAM derived products is 5'-Deoxyadenosine. Since 5'-dA has been demonstrated to be an inhibitor of radical SAM enzymes; a pathway for removing this product must be present. We propose here that DadD is involved in the recycling of 5'-Deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'-deoxyinosine is further metabolized to deoxyhexoses used for the biosynthesis of aromatic amino acids in methanogens.