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3'-O-butanoyl-5-fluoro-2'-deoxyuridine is a chemical compound that belongs to the class of nucleoside analogs, specifically a derivative of the naturally occurring nucleoside thymidine. 3'-O-butanoyl-5-fluoro-2'-deoxyuridine is characterized by the presence of a 5-fluoro group, which replaces the hydrogen atom at the 5-position of the uracil base, and a butanoyl group attached to the 3' position of the deoxyribose sugar moiety. The butanoyl group is a four-carbon acyl chain that contributes to the lipophilic nature of the molecule, potentially enhancing its cellular uptake. The fluorination at the 5-position can modulate the electronic properties of the molecule, affecting its interactions with enzymes and other biomolecules. This chemical modification may lead to altered biological activities compared to the parent compound, making it a subject of interest in medicinal chemistry for potential therapeutic applications, such as antiviral or anticancer drugs.

7207-60-5

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7207-60-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7207-60-5 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,2,0 and 7 respectively; the second part has 2 digits, 6 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 7207-60:
(6*7)+(5*2)+(4*0)+(3*7)+(2*6)+(1*0)=85
85 % 10 = 5
So 7207-60-5 is a valid CAS Registry Number.

7207-60-5Downstream Products

7207-60-5Relevant academic research and scientific papers

Regioselective acylation of nucleosides catalyzed by candida antarctica lipase B: Enzyme substrate recognition

Li, Ning,Zong, Min-Hua,Ma, Ding

, p. 5375 - 5378 (2008)

The substrate recognition of Candida antarctica lipase B (CAL-B) in the acylation of nucleosides was revealed through rational substrate engineering for the first time. CAL-B displayed lower activities and excellent 5′-regioselectivities (94 to >99%) in t

Regioselective acylation of nucleosides and their analogs catalyzed by Pseudomonas cepacia lipase: enzyme substrate recognition

Li, Ning,Zong, Min-Hua,Ma, Ding

supporting information; experimental part, p. 1063 - 1068 (2009/04/11)

The substrate recognition of Pseudomonas cepacia lipase in the acylation of nucleosides was investigated by means of rational substrate engineering for the first time. P. cepacia lipase displayed excellent 3′-regioselectivities (96 to >99%) in the lauroyl

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