Monitoring the Changes in the Microbial Dynamics
of Calcareous Soil with the Amendment
of Stabilized and Dried Sewage Sludge
in Mediterranean Region of Turkey

Tavali, İsmail Emrah; Orman, S.; Ozgur, Aylin; Uz, İlker; Sulaman, Saira

doi:10.15244/pjoes/135613

Cited by 2 publications

(2 citation statements)

References 29 publications

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“…[7][8][9][10] Therefore, the synthesis of safe as well as effective urease inhibitors constitutes a vital region of research for both agriculture and pharmaceutical applications. [11,12] All the ureases that originate from different sources display similar mechanisms of action due to common tertiary structures that are highly conserved and the sequences of amino acids in the enzyme's active site. Among many of the ureases, jack bean (Canavalia ensiformis) urease is the bestcharacterized and widely used in inhibition studies.…”

Section: Introductionmentioning

confidence: 99%

“…In addition, ureases are involved in acute pyelonephritis, urolithiasis, infection‐induced reactive arthritis, and infection by Yersinia enterocolitica and Proteus mirabilis [7–10] . Therefore, the synthesis of safe as well as effective urease inhibitors constitutes a vital region of research for both agriculture and pharmaceutical applications [11,12] . All the ureases that originate from different sources display similar mechanisms of action due to common tertiary structures that are highly conserved and the sequences of amino acids in the enzyme's active site.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Design, Synthesis, Characterization and Computational Studies of Mannich Bases Oxadiazole Derivatives as New Class of Jack Bean Urease Inhibitors

Mutahir

Khan

Almehizia

et al. 2023

Chemistry & Biodiversity

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Mannich bases consisting of 1,3,4‐oxadiazole‐2‐thione (3 a–3 l) bearing various substituents were synthesized and found potent jack bean urease inhibitors. The prepared compounds showed significantly good inhibitory activities with IC50 values from 9.45±0.05 to 267.42±0.23 μM. The compound 3 k containing 4‐chlorophenyl (−R) and 4‐hydroxyphenyl (−R′) was most active with IC50 9.45±0.05 μM followed by 3 e (IC50 22.52±0.15 μM) in which −R was phenyl and −R′ was isopropyl group. However, when both −R and −R′ were either 4‐chlorophenyl groups (3 l) or only −R′ was 4‐nitrophenyl (3 i), both compounds were found inactive. The detailed binding affinities of the produced compounds with protein were explored through molecular docking and data‐supported in‐vitro enzyme inhibition profiles. Drug likeness was confirmed by in silico ADME investigations and molecular orbital analysis (HOMO‐LUMO) and electrostatic potential maps were got from DFT calculations. ESP maps exposed that there are two potential binding sites with the most positive and most negative parts.

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