scholarly journals In Vitro and In Silico Characterization of Kurarinone as a Dopamine D1A Receptor Antagonist and D2L and D4 Receptor Agonist

ACS Omega ◽  
2021 ◽  
Author(s):  
Ritu Prajapati ◽  
Su Hui Seong ◽  
Pradeep Paudel ◽  
Se Eun Park ◽  
Hyun Ah Jung ◽  
...  
2017 ◽  
Vol 362 (2) ◽  
pp. 287-295 ◽  
Author(s):  
Carsten Theodor Beuckmann ◽  
Michiyuki Suzuki ◽  
Takashi Ueno ◽  
Kazuya Nagaoka ◽  
Tohru Arai ◽  
...  

Author(s):  
Markus Boel ◽  
Oscar J. Abilez ◽  
Ahmed N Assar ◽  
Christopher K. Zarins ◽  
Ellen Kuhl

2019 ◽  
Vol 13 (2) ◽  
pp. 159-170 ◽  
Author(s):  
Vishal Ahuja ◽  
Aashima Sharma ◽  
Ranju Kumari Rathour ◽  
Vaishali Sharma ◽  
Nidhi Rana ◽  
...  

Background: Lignocellulosic residues generated by various anthropogenic activities can be a potential raw material for many commercial products such as biofuels, organic acids and nutraceuticals including xylitol. Xylitol is a low-calorie nutritive sweetener for diabetic patients. Microbial production of xylitol can be helpful in overcoming the drawbacks of traditional chemical production process and lowring cost of production. Objective: Designing efficient production process needs the characterization of required enzyme/s. Hence current work was focused on in-vitro and in-silico characterization of xylose reductase from Emericella nidulans. Methods: Xylose reductase from one of the hyper-producer isolates, Emericella nidulans Xlt-11 was used for in-vitro characterization. For in-silico characterization, XR sequence (Accession No: Q5BGA7) was used. Results: Xylose reductase from various microorganisms has been studied but the quest for better enzymes, their stability at higher temperature and pH still continues. Xylose reductase from Emericella nidulans Xlt-11 was found NADH dependent and utilizes xylose as its sole substrate for xylitol production. In comparison to whole cells, enzyme exhibited higher enzyme activity at lower cofactor concentration and could tolerate higher substrate concentration. Thermal deactivation profile showed that whole cell catalysts were more stable than enzyme at higher temperature. In-silico analysis of XR sequence from Emericella nidulans (Accession No: Q5BGA7) suggested that the structure was dominated by random coiling. Enzyme sequences have conserved active site with net negative charge and PI value in acidic pH range. Conclusion: Current investigation supported the enzyme’s specific application i.e. bioconversion of xylose to xylitol due to its higher selectivity. In-silico analysis may provide significant structural and physiological information for modifications and improved stability.


2017 ◽  
Vol 15 ◽  
pp. 55-62 ◽  
Author(s):  
Laura Marcela Palma Medina ◽  
Diana Catalina Ardila ◽  
María Mercedes Zambrano ◽  
Silvia Restrepo ◽  
Andrés Fernando González Barrios

3 Biotech ◽  
2018 ◽  
Vol 8 (3) ◽  
Author(s):  
Bruna Leite Sufiate ◽  
Filippe Elias de Freitas Soares ◽  
Samara Silveira Moreira ◽  
Angélica de Souza Gouveia ◽  
Evandro Ferreira Cardoso ◽  
...  

2008 ◽  
Vol 21 (12) ◽  
pp. 2289-2299 ◽  
Author(s):  
James R. Roede ◽  
David L. Carbone ◽  
Jonathan A. Doorn ◽  
Oleg V. Kirichenko ◽  
Philip Reigan ◽  
...  

Author(s):  
Mohammad Mahdi Hajjari ◽  
Mohammad-Taghi Golmakani ◽  
Niloufar Sharif ◽  
Mehrdad Niakousari

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