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37987-27-2

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37987-27-2 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 37987-27-2 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 3,7,9,8 and 7 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 37987-27:
(7*3)+(6*7)+(5*9)+(4*8)+(3*7)+(2*2)+(1*7)=172
172 % 10 = 2
So 37987-27-2 is a valid CAS Registry Number.

37987-27-2Relevant articles and documents

Regioselectivity of Cobalamin-Dependent Methyltransferase Can Be Tuned by Reaction Conditions and Substrate

Pompei, Simona,Grimm, Christopher,Farnberger, Judith E.,Schober, Lukas,Kroutil, Wolfgang

, p. 5977 - 5983 (2020/10/06)

Regioselective reactions represent a significant challenge for organic chemistry. Here the regioselective methylation of a single hydroxy group of 4-substituted catechols was investigated employing the cobalamin-dependent methyltransferase from Desulfitobacterium hafniense. Catechols substituted in position four were methylated either in meta- or para-position to the substituent depending whether the substituent was polar or apolar. While the biocatalytic cobalamin dependent methylation was meta-selective with 4-substituted catechols bearing hydrophilic groups, it was para-selective for hydrophobic substituents. Furthermore, the presence of water miscible co-solvents had a clear improving influence, whereby THF turned out to enable the formation of a single regioisomer in selected cases. Finally, it was found that also the pH led to an enhancement of regioselectivity for the cases investigated.

ANTI-HIV COMPOUNDS

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Paragraph 0232, (2016/07/05)

This invention provides, among other things, tetrahydroisoquinolines useful for treating viral infections, pharmaceutical formulations containing such compounds, as well as methods of inhibiting the replication of a virus, such as HIV, or treating a disease, such as AIDS.

Galactose oxidase models: Solution chemistry, and phenoxyl radical generation mediated by the copper status

Michel, Fabien,Thomas, Fabrice,Hamman, Sylvain,Saint-Aman, Eric,Bucher, Christophe,Pierre, Jean-Louis

, p. 4115 - 4125 (2007/10/03)

Galactose oxidase (GO) is an enzyme that catalyzes two-electron oxidations. Its active site contains a copper atom coordinated to a tyrosyl radical, the biogenesis of which requires copper and dioxygen. We have recently studied the properties of electrochemically generated mononuclear CuII-phenoxyl radical systems as model compounds of GO. We present here the solution chemistry of these ligands under various copper and dioxygen statuses: N3O ligands first chelate CuII, leading, in the presence of base, to [CuII(ligand)(CH3CN)]+ complexes (ortho-tert-butylated ligands) or [(CuII)2(ligand) 2]2+ complexes (orthomethoxylated ligands). Excess copper-(II) then oxidizes the complex to the corresponding mononuclear Cu II-phenoxyl radical species. N2O2 tripodal ligands. in the presence of copper(II), afford directly a copper(II)-phenoxyl radical species. Addition of more than two molar equivalents of copper( II) affords a CuII-bis(phenoxyl) diradical species. The donor set of the ligand directs the reaction towards comproportionation for ligands possessing an N3O donor set, while disproportionation is observed for ligands possessing an N2O2 donor set. These results are discussed in the light of recent results concerning the self-processing of GO. A path involving copper(II) disproportionation is proposed for oxidation of the crosslinked tyrosinate of GO, supporting the fact that both copper(I) and copper(II) activate the enzyme.

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