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• W2993310648 abstract "DT-Diaphorase (DTD) belonging to the oxidoreductase family, is among the most important enzymes and is of great significance in present-day biotechnology. Also, it has potential applications in glucose and pyruvate biosensors. Another important role of the DTD enzyme is in the detection of Phenylketonuria disease. According to the above demands, at first, we tried to study molecular cloning and production of recombinant DTD in E. coli BL21 strain. We have successfully cloned, expressed, and purified functionally active diaphorase. The amount of enzyme was increased in 10-h using IPTG induction, and the recombinant protein was purified by Ni-NTA agarose affinity chromatography. After that, the kinetic and thermodynamic parameters of the enzyme, optimum temperature and pH were also investigated to find more in-depth information. In the end, to represent the connections between the structures and function of this enzyme, the molecular dynamics simulations have been considered at two temperatures in which DTD had maximum and minimum activity (310 and 293 K, respectively). The results of MD simulations indicated that the interaction between NADH with phenylalanine 232 residue at 310 K is more severe than other residues. So, to investigate the interaction details of NADH/PHE 232 the DFT calculations were done." @default.
• W2993310648 created "2019-12-13" @default.
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• W2993310648 date "2020-01-01" @default.
• W2993310648 modified "2023-09-24" @default.
• W2993310648 title "From in vitro to in silico: Modeling and recombinant production of DT-Diaphorase enzyme" @default.
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• W2993310648 doi "https://doi.org/10.1016/j.ijbiomac.2019.12.029" @default.
• W2993310648 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31812741" @default.
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