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126799-84-6

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126799-84-6 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 126799-84-6 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,6,7,9 and 9 respectively; the second part has 2 digits, 8 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 126799-84:
(8*1)+(7*2)+(6*6)+(5*7)+(4*9)+(3*9)+(2*8)+(1*4)=176
176 % 10 = 6
So 126799-84-6 is a valid CAS Registry Number.

126799-84-6Relevant articles and documents

A Photoregulated Racemase Mimic

Saha, Monochura,Hossain, Munshi Sahid,Bandyopadhyay, Subhajit

, p. 5220 - 5224 (2021)

The racemase enzymes convert L-amino acids to their D-isomer. The reaction proceeds through a stepwise deprotonation–reprotonation mechanism that is assisted by a pyridoxal phosphate (PLP) coenzyme. This work reports a PLP–photoswitch–imidazole triad where the racemization reaction can be controlled by light by tweaking the distance between the basic residue and the reaction centre.

Design, synthesis, and evaluation of metronidazole-1,2,3-triazole derivatives as potent urease inhibitors

Rezaei, Elham Babazadeh,Abedinifar, Fahimeh,Azizian, Homa,Montazer, Mohammad Nazari,Asadi, Mehdi,Hosseini, Samanesadat,Sepehri, Saghi,Mohammadi-Khanaposhtani, Maryam,Biglar, Mahmood,Larijani, Bagher,Amanlou, Massoud,Mahdavi, Mohammad

, p. 4217 - 4226 (2021/04/26)

A new series of metronidazole-1,2,3-triazole derivatives 6a–o was synthesized and evaluated as Helicobacter pylori urease inhibitors. All the synthesized compounds were more potent than standard inhibitor thiourea against urease. Among the synthesized compounds, compound 6f (IC50 = 1.975 ± 0.25?μM) with inhibitory activity around 11-fols more than thiourea (IC50 = 22.00 ± 0.14?μM) was the most potent compound. Kinetic study of this compound revealed that compound 6f inhibited urease in an uncompetitive mode. Based on molecular modeling study, compound 6f pointed toward the bi-nickel center and stabilized by H-bond and T-shape π–π hydrophobic interactions with the critical residues His492 and Asp633. Moreover, it anchored to the helix-turn-helix motif in the active site cavity through interaction with His593 and Arg609. Consequently, it proposed that compound 6f through stabilization of active site flap inhibited urease activity.

Synthesis of 1,2,3,triazole modified analogues of hydrochlorothiazide via click chemistry approach and in-vitro α-glucosidase enzyme inhibition studies

Baheej, M. A. A.,Choudhary, M. Iqbal,Haniffa, Haroon M.,Iqbal, Shazia,Rizvi, Fazila,Siddiqui, Hina,Ullah, Saeed,Wahab, Atia-tul

, (2021/10/07)

The current study was aimed to discover potent inhibitors of α-glucosidase enzyme. A 25 membered library of new 1,2,3-triazole derivatives of hydrochlorothiazide (1) (HCTZ, a diuretic drug also being used for the treatment of high blood pressure) was synt

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