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59756-83-1

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59756-83-1 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 59756-83-1 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 5,9,7,5 and 6 respectively; the second part has 2 digits, 8 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 59756-83:
(7*5)+(6*9)+(5*7)+(4*5)+(3*6)+(2*8)+(1*3)=181
181 % 10 = 1
So 59756-83-1 is a valid CAS Registry Number.

59756-83-1Relevant articles and documents

Design, synthesis, and biological evaluation of oxazolidone derivatives as highly potent N-acylethanolamine acid amidase (NAAA) inhibitors

Ren, Jie,Li, Yuhang,Ke, Hongwei,Li, Yanting,Yang, Longhe,Yu, Helin,Huang, Rui,Lu, Canzhong,Qiu, Yan

, p. 12455 - 12463 (2017/03/11)

N-Acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme that catalyzes the hydrolysis of endogenous fatty acid ethanolamides (FAEs), such as N-palmitoylethanolamide (PEA). PEA exhibits anti-inflammatory and analgesic activities by engaging peroxisome proliferator-activated receptor α (PPAR-α). Preventing PEA degradation by inhibition of NAAA has been proposed as a novel strategy for the treatment of inflammation and pain. In the present study, we reported the discovery of the oxazolidone derivative as a novel scaffold for NAAA inhibitors, and studied the structure-activity relationship (SAR) by modification of the side chain and terminal lipophilic substituents. The results showed that the link chain length of C5, straight and saturated linkages were the preferred shape patterns for NAAA inhibition. Several nanomolar NAAA inhibitors were described, including 2f, 3h, 3i and 3j with IC50 values of 270 nM, 150 nM, 100 nM and 190 nM, respectively. Enzymatic degradation studies suggested that 2f inhibited NAAA in a selective, noncompetitive and reversible pattern. Moreover, 2f showed high anti-inflammatory and analgesic activities after systemic and oral administration.

Enantioselective Oxidative Aerobic Dealkylation of N-Ethyl Benzylisoquinolines by Employing the Berberine Bridge Enzyme

Gandomkar, Somayyeh,Fischereder, Eva-Maria,Schrittwieser, Joerg H.,Wallner, Silvia,Habibi, Zohreh,Macheroux, Peter,Kroutil, Wolfgang

supporting information, p. 15051 - 15054 (2016/01/25)

N-Dealkylation methods are well described for organic chemistry and the reaction is known in nature and drug metabolism; however, to our knowledge, enantioselective N-dealkylation has not been yet reported. In this study, exclusively the (S)-enantiomers o

Biocatalytic enantioselective oxidative C-C coupling by aerobic C-H activation

Schrittwieser, Joerg H.,Resch, Verena,Sattler, Johann H.,Lienhart, Wolf-Dieter,Durchschein, Katharina,Winkler, Andreas,Gruber, Karl,MacHeroux, Peter,Kroutil, Wolfgang

supporting information; experimental part, p. 1068 - 1071 (2011/04/22)

Bridging the gap: The berberine bridge enzyme (BBE) was employed for the first preparative oxidative biocatalytic C-C coupling that leads to a new intramolecular bond. This unique transformation requires O2 as sole stoichiometric oxidant and gives access to novel optically pure (S)-berbine 2 and (R)-1-benzyl-1,2,3,4-tetrahydroisoquinoline 1 alkaloid derivatives by kinetic resolution.

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