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Merck

D1771

Sigma-Aldrich

5'-脱氧腺苷

methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase substrate

别名:

5′-dAdo

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About This Item

经验公式(希尔记法):
C10H13N5O3
CAS号:
分子量:
251.24
MDL號碼:
分類程式碼代碼:
41106305
PubChem物質ID:
NACRES:
NA.51

生物源

synthetic (organic)

品質等級

化驗

≥98% (TLC)

形狀

powder

溶解度

hot water: 19.60-20.40 mg/mL, clear, colorless

儲存溫度

2-8°C

SMILES 字串

C[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23

InChI

1S/C10H13N5O3/c1-4-6(16)7(17)10(18-4)15-3-14-5-8(11)12-2-13-9(5)15/h2-4,6-7,10,16-17H,1H3,(H2,11,12,13)/t4-,6-,7-,10-/m1/s1

InChI 密鑰

XGYIMTFOTBMPFP-KQYNXXCUSA-N

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應用

5′-脱氧腺苷已用于:
  • 作为质谱中的标准品
  • 、作为筛选胸苷磷酸化酶活性的抑制剂
  • 、作为 5′-脱氧腺苷脱氨酶(DadD)试验的底物

生化/生理作用

5′-脱氧腺苷是微生物中甲基硫代腺苷/ S -腺苷同型半胱氨酸 (MTA/SAH)核苷酶的底物。 5′-脱氧腺苷是 S -腺苷甲硫氨酸(SAM)裂解的副产物。5′ 高水平脱氧腺苷抑制SAM 依赖性酶。它还抑制生物素合成酶(BioB)和硫辛酸合成酶(LipA)。

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


分析证书(COA)

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The nucleoside derivative 5?-O-trityl-inosine (KIN59) suppresses thymidine phosphorylase-triggered angiogenesis via a noncompetitive mechanism of action
Liekens S, et al.
Test, 279(28), 29598-29605 (2004)
Kenichi Yokoyama et al.
Biochemistry, 47(34), 8950-8960 (2008-08-05)
BtrN is a radical SAM ( S-adenosyl- l-methionine) enzyme that catalyzes the oxidation of 2-deoxy- scyllo-inosamine (DOIA) into 3-amino-2,3-dideoxy- scyllo-inosose (amino-DOI) during the biosynthesis of 2-deoxystreptamine (DOS) in the butirosin producer Bacillus circulans. Recently, we have shown that BtrN catalyzes
Charles J Walsby et al.
Inorganic chemistry, 44(4), 727-741 (2005-04-30)
Electron paramagnetic resonance (EPR), electron-nuclear double resonance (ENDOR), and Mössbauer spectroscopies and other physical methods have provided important new insights into the radical-SAM superfamily of proteins, which use iron-sulfur clusters and S-adenosylmethionine to initiate H atom abstraction reactions. This remarkable
Joseph T Jarrett
Current opinion in chemical biology, 7(2), 174-182 (2003-04-26)
Adenosylmethionine-dependent radical enzymes provide a novel mechanism for generating the highly oxidizing 5'-deoxyadenosyl radical in an anaerobic reducing environment. Recent studies suggest a unique covalent interaction between adenosylmethionine and a catalytic iron-sulfur cluster that may promote inner-sphere electron transfer to
Gunhild Layer et al.
Current opinion in chemical biology, 8(5), 468-476 (2004-09-29)
'Radical SAM' enzymes juxtapose a [4Fe-4S] cluster and S-adenosyl-l-methionine (SAM) to generate catalytic 5'-deoxyadenosyl radicals. The crystal structures of oxygen-independent coproporphyrinogen III oxidase HemN and biotin synthase reveal the positioning of both cofactors with respect to each other and relative

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